Comments
Description
Transcript
Number 35
Essays of an Information Scientist, p254, 1979-80 Current Contents, #35, p.5-14, August 27, 1979 Moat-Cited Biochemfsq Number 35 Adck and of the 1%0s. 2. ~OkWf!Xr Bicdogy August 27, 1979 Recently we listed the most-cited physical sciences articles of the 1960s. 1 To continue our discussion of that decade’s scientific literature we have now compifed a list of the most-cited biochemistry and molecular biology papers. These lists of most-cited articles are selected by sorting and ranking the Science Citation Index@ (SCP) files for the 18-year period from 1%1 to 1978. Over seventy-one million citations to authored items are included in the SC1 data base for those years.z About 11 million of those citations are to papers published during the 1960s. I estimate that over 60,000 biochemistry papers were published during that time.3 To select a limited number of papers from this massive volume of publication may seem like a futife exercise. Nevertheless, by identifying this sample I think we learn quite a bit about the main directions and logistics of biochemical research in the 60s. I do not wish to suggest that these articles were the most “important” intellectual contributions to biochemistry in that decade. Many of the papers would qualify as such, but many authors have indicated to us that they published other papers that are more representative of their best work. Nevertheless, 1 find it hard to believe that it is a coincidence that these authors have so often been recognized by their peers. Put it this way—the authors of highly cited papers also tend to publish other wellcited papers. 254 In providing the frequency of citation I do not suggest that this is an indicator of relative “value. ” In the case of a theoretical paper it may be an indication of impact or influence. For a widely used method paper it may simply indicate just that. Citation data may be the only convenient means of determining the impact of a new methodology. Others might prefer to use the annual sales of a particular biochemical reagent or instrument. If nothing else, citation frequency does allow us to make comparisons between the kinds and amounts of activities symbolized by the articles involved. I hope that the alphabetical arrangement by first author under each category will discourage invidious comparisons. There are 101 articles listed in Figure 1 which follows this editorial. Originally, I intended to limit the study to 100 articles. Because both parts of Omura’s work on liver microsomes appear on the list, I decided to add one more paper. Every paper on the list was cited more than 564 times during the period 1%1-78. Thirty-nine were cited more than 1000 times and 11 more than 2000 times. The average paper received 1294 citations. This means that it was cited at least 72 times per year. You can better appreciate the significance of this number when you consider that the average article published in a journal covered by SCI during this period received 3.28 citations. However, for biochemistry papers one would expect this figure to be doubled because the average biochemistry paper now contains twice as many references as the average SCI paper. The papers were published in the 25 journals lis’ed in Table 1. Fifty-two were publiihed in five journals: Journal of Molecular Biology, Journal of Biological Chemistry, Proceedings of the National Academy of Sciences US, Biochemical Journal. and Analytical Biochemistry. None of this will surprise anyone familiar with the field. Tnbta I: Journals that pubfisbed the most cited 1%0s articles fisted in Figure 1. according to number of articles. No. 01 Ardcles Joamal J. M(,I Bid 14 J. JJiol. Chcm 12 Proc Acad Sci. US Nat Biochmn Anal. 9 9 J n Bmchem JJwchemtsmy h Science h Arch. B!ophys. Acts 6 5 Biophys. Rcs. Commun. 3 Ehochcm. Biophys. Biochcm 5 Nature Bwchem 3 J L,pid Res. Ann. NY Acad. J titw?chem AcIa Chem Anal Sci. Cymchem. Scartd 1 ZetI I Bt<q)hys. J Eur I I Chcrn Biochcm. 2 2 I 1 Bncxhem J Am Chcm J Am Oil Chem. Sex. SW. I 1 J Btochem —Tokyo I J. Cd ! Bnd. J Chromatography J M<)l I Pharr(w,col. - Prcdcccwm of Eur. j. JSiochcm, However, thw is hinddght judgment. If we consider that the fiit issue of the Journal of Molecular Biology appeared in 1959, and the fiit issue of Analytical Biochemistry in 1960, it seems unusual that they accounted for such a large proportion of the most-cited papem of the 1960s. I can well remember when Kurt lacoby and Roselle Coviello started A nalyticai Biochemistry for Academic Press with the late Dr. Alvin Nason as its founding editor.q I know that he and Jim Barsky, who joined the editorial board of Academic Press in 1%3, took special pride in the rapid success of this journal. Dr. N.O. Kaplan of the University of Caliiomia at San D~ego, co-chairman of the editorial committee of Analytica{ Biochemistry, attributes its success to the fact that it concentrates solely on publishing methodology papers. Furthermore, the papers are reviewed quite carefully, and only those describing novel methods or developments are accepted. s I hasten to point out that its impact factor is not SignKlcantly different from other high impact journals. Therefore, most methodology papers it published did not achieve such high use. Methodology papers often appear among articles that are most-cited, but not all methodology papers are heavily cited. Dr. S. Brenner of the Medcal Research Council of the UK was one of the founding editors of the Journal of Molecular Biology. He says the succes+ of the journal can be accounted for relatively simply. The number of leading figures in the field was not large in 1959. This made it possible for the editors to contact most of them directly. So, the journal was founded with the support of most of the people who were active and interested in the field. Subsequently, they all published in Journal of Molecular Biology. 6 But one could say this about many other less successful journals. The widespread and rapid impact of molecular biology is also part of the story. Certainly the Jouma! of Molecular Biology was there at the right time. But I’ve often wondered why it took so long after the Watson-Crick paper7 for this to occur. Biochemistry, published by the American Chemical Society, was started in 1%4. The six papers it contributed are equivalent to nine or ten from a journal established before 1960. This journal, like most of the journals on this list, is a high impact journal. Seventy-three papers on the fist have two or more authors. Forty-two have two, 20 have three, and nine have four. 255 one paper has six authors and one has eight. The total number of authors appearing on the list is 222. OnJy 28 papers were written by one author. This is quite a change from the situation in the forties.B Ail papers on the list are written in English, except H. Wagner’s paper in German on the separation of phosphofipids by chromatography. Thk was publiihed in Biochemische Zeitschn~t, the predecessor to the European Journal of Biochemistry. Sixty-three institutions (shown in Table 2) are represented on the fist. Just nine institutions account for 92 of the 222 authors. The list is dominated by American laboratories, which account for 39 of the 63 research institutions. The United Kingdom follows with nine, Sweden with six, and Australia and Japan are represented by two institutions each. France, the Federal Republic of Germany, Italy, Switzerland, and Taiwan are represented by one each. Eighteen authors have two or more papers on the list. B.N. Ames, P. Andrews, J.P. Changeux, W .W. Cleland, P. Doty, A.D. Hershey, F. Jacob, C.B. Lauren, S. Moore, M. Nirenberg, T. Omura, K.A. Piez, R.A. Reisfeld, R. Sate, and S. Spiegelman each wrote two papers. R.J. Britten, J. Marmur, and J. Monod each wrote three papers. Thirteen papers were authored by eleven Nobel laureates. E.L. Tatum was awarded the prize for medicine in 1958 for his work on genes and heredity. The 1958 prize for chemistry went to F. Sanger for hk work on the chemical composition of insulin. M. F. Perutz received the 1962 chemistry prize for defining the structure of proteins. F. Jacob and J. Monod shared the 1965 medicine prize for their study of cellular mechanisms controlling enzymes and virus synthesis. The 1968 prize for medicine was awarded to M.W. Nirenberg and R. W. Honey for their work on the genetic code and enzymes. A. D. Hershey was awarded the f969 medicine prize for his investigation of the genetic structure of viruses. The 1972 prize for chemistry was awarded to S. Moore, W.H. Stein, and C.B. Anfinsen for their work on enzymes. In a study I did with Irv Sher in 1965 we showed that articles written by Nobel laureates were highly cited long before they received the prize.g That is why we believed citation data had some forecasting value. This is true for eight of the eleven Nobel laureates on the list. E.L. Tatum received the prize in 19S8. He appeared on our fiit of most-cited biomedicine papers of the 19-40s, years before he was awarded the Nobel Prize. 10 However, his most-cited paper was published in 1%2. The same is true of F. Sanger. He received the prize in 1958 and his most-cited paper was pubfished in 1965. Sanger appeared on our list of most-cited biochemistry papers of the 1940s.s Lastly, M.F. Perutz received the prize in 1%2. His most-cited paper appeared in 1968. Thus, as Harriet Zuckermanl I has pointed out, many Nobel laureates continue to make highly cited contributions to science in the years before and after their award. Ten of the articles listed have appeared as Citation Classics in Current Contents@ (C@). Since most CC readers are familiar wit h this feature, I wifl not elaborate any further. On the whole, methodology papers dominate the lit, accounting for 68 of the 101 articles. Unquestionably, methods are the backbone of scientific research. David Gillespie of the National Cancer Institute suggests two reasons why a particular method paper is highfy cited. He says, “The distinction between a classic and a quickly outmoded method lies in the ability of the investigators to see the uses to which the method will be put... and, as importantly, to take heed of the little irregularities that lead to significant improvemerits. ”lz It is important to note that well-cited methodology papers are in a special class. While most methodology papers do not fare better than other papers, the most successful ones are more heavily 256 Tabla 2. Insritu[ional affiliations of most-cited 196CJSarticles. according authors of the to number Mt. Sinai Hosp. INCW York, of 4 NY I Cell Res. Lab. 2 Dt+ 2 authors. Neuropath<d Oak Ridge Nal, Lab. (Oak 4 Ridge, TN) Osaka [Iniw. (Osaka, No. lnsmu!e Arthritis 01 National Heart Institute National 2 MA I II 3 Med. 2 Sch. COU.CII. [Inn MRC. (New York. Washmgbm IWashingmn, TerresmialMagnetism 5 Dep!. Gcnet 4 Harbor, Cold Spring Enaland I Ph!sburgh lPiusburgh. PA I (Cambridge. Jowa (lOWa CIIY, IA) 2 Uni,. Ken[ucky 2 Uni*. Lund (Sweden) 2 Univ. Southampton 2 ILexmaton. Skxkholm. Uppsala (Uppsala, Virginia Sch (Charlottesville. b NY} Microbiol. 4 Ophthalmol. I Howard Dep. Bmchem. 1 s Last. Technol. N. W Columbta Church Lab. Chem. lJmv. (New York. Biol. 2 Dcpt M#crobiol. J Wm.. Dept Mcd 5 (Ithaca, NY) 4 Bmchem 5 5 Cahfomia Davis. Dcpt Food SCI. & Tech 3 Davis. Dept Bic~h. & Biophy$ 2 IL) I Waltham. MA) Med Dcpl B],)phy, 1 Mcc’<>llum Pratt [ml I I ( Stmkh<,lm. Rc$. (La.sanne, Pharmaccut (Sendai, Cancer Swiwerland I Sch Japan I (Inw Adelaide (Austrabal Ilniv Colorado Mcd (Imv M!ami 4 (Inii. Rochester Dentistry Ctr COI” 5 4 D.pl ImI Edinburgh John* Hopkins I Bab8m<,rc. Ml) I Taiwan I 1 kxpenmcn!al IFhlder, 4 Med. I lcalyl (Taipei. NY) (Inn Ctty of Hupc Med. Ctr. IDuarce. CA I Sch I Hosp Blood C1r. Med. Tohoku C,ty (d New York Illinots (Ilrbana. Nobel SWISS lnsl Public Health Res. Inst. Brandms (km BcaMy Swedenl I Coil. Univ. (New York. 5 Unw. Res.. Chesmr Englandl Taiwan New York Massachusetts Inst. Techno! (Cambridge. MA I [Inn [nst. Cancer Nat I Inst. FL) ISI. Rcgma Elena iR,,me, 5 Biihcm. Cornell Hughes Mcd. I London, 3 NY} Dqn. 2 1 Res. Inst., Royal Cancer 2 DIV. Bid 2 NY) DepI. {Miami. 2 2 CT) Etnstein C<d!. Mcd Dep(. (Pasadena. CA} Sweden) Mcd Chalmers Inst. Tcchmd IGothe”bq. Sweden) Cdifomia Inst VA I (New Haven. (New York. lNew York, Wcnner-Gren Sweden ) Univ. Albert KY I kngiand I [l”iv. MI) Sch. Med. Glasgow {Glasguw, Yale Univ. Sco[lmdl 2 (Inm 7 b Sta!c Umv. lEasI Lansing, Englandl hb. Biochcm. 7 3 Sch. Med. 2 Res. Untv Univ. 4 & Nutrit. Rr$. (1nit Auwrabal ISmckhcdm. DCPI. Biochem 2 Cambridge ( !iouthampton. NY Inst. Pastcurl Pans. France) NYU 9 DC) Dept. M,chigan 10 2 2 Cancer Mcd Sch. Med. Dcpt I NY I Camegielnst. Ins! Hosp Physiol. +@d Swedenl Englandl (Melbourne. Univ. 3 NC) Dairytng (London. 9 Harwcll, 3 PA I {Stockholm. S!. Vmccn! [Ire.. Iu UK 3 NY) Mary’s Cambridge, England Rockefeller (Rye. b Cbcm. Biol. Labs. Re! Inst Sloan-Kettering St (Phda.. Ctr. (Durham. Jnst. Res. IShmficld. 2 MRC. Med Karobnska & Inlcctkous D]s.sasss NY} Res. Labs NJ) Pennsylvania Namma[ un spcctfied Haward Unm (Cambridge. Depl. [Inn Instimtc of Allergy 2 I Nat. Lab. (Ilpton. Duke llIIN 4 lnsmute Biochcm. Stanford [Ini$. Sch. Med. [1”,,. Munich (M””,ch, FRGI 2 Cancer Nahonal Btochem. 4 WI I I Sharp & Dohmc IRahway. Instiru#c of Dental Research National Dcpt Merck n n ( Madison, Lab. .& Depl. Aarkcuhurc Brookha$en DISCascs Unw. W iscomi” Biophys & Metabolic 4 4 Agricdmre Cdl. 2b Institutes of Heabh Natwnd Med. { III), Authon Instlkulsm National I IS DcpI of Japan) (M,ami. Sch NY I TN) I I E“gla”d) H(,lc Marim (W<)MIS H,de, 1 Med. {Rochester. (Bcckhenham, I FLI” [lniv. Tennessee (Knon\dlc wellc,,nw Rm, Labs Woods I {Scotland) B,,)l I Lab MA9 . Sectmd afltl,ali,m for a smgl. e..th<,red paper electrophoresis and the paper by Weber and Osborn on gel electrophoresis, among others, bring out certain points about citation frequencies above the 564 threshold. It should be clear that no greater intellectual significance should be attributed to these papers than to others on the list simply because they were cited more than 9,0LXI times. Many people have to be reminded of this lest they take citation counts at face value. However, the economic and policy implications of such widespread use of a new technique does tell science administrators how to make research more efficient. I should think that any future discovery that would d~place these methods could have enormous impact. The paper by Weber and Osbom is in fact the most-cited on the list. “The reliability of molecular weight determinations by dodecyl sulfate-polyacryIamide gel electrophoresis” was cited 9,509” times in just ten years since its publication in 1%9. The authors experimentally confirm that electrophoresis can accurately determine the molecular weights of polypeptide protein chains. There are in fact only a smalf number of papers or books in the entire history of science cited more than 2,000 times. The classic example is the Lowry method for protein determination. What is not clear here is why people continue to cite those methods explicitly and not cite others. Seventeen papers d~cuss one or more aspect of chromatography. Clearly large numbers of scientists need to estimate the molecular weights of proteins, and many use the sephadex gel-filtration method described by Andrews. Five papers deal with centrifugation/sedimentation techniques which are instrumental in studies of protein synthesis, where RNA molecules of different size and weight must be distinguished. The remaining 20 papers cover miscellaneous topics and methods including quantitative estimations of cited than theoretical papers. Thus it would be expected that they would dominate a list that represents about one out of every six hundred published in biochemistry during the 60s.3 As you can see, the list has been divided into several categories-nucleic acids, protein structure, enzymology, electrophoresis, chromatography, centrifugation/sedimentation, and miscellaneous. These categories are not meant to be definitive. A simple arrangement by journal might have been equally useful. The titles of most papers provide a better capsule description than I could provide in the space available. The rapid growth of molecular biology is reflected in the first group of 25 papers on the nucleic acids, DNA, and RNA. Seven deal with the gene’s role in protein and RNA synthesis. The Jacob and Monod paper is a good example of a review article that contains new and important ideas not apparent in the sources under review. ”rn this paper they suggested the now familiar concept of a messenger RNA. For this Jacob and Monod were awarded the Nobel prize in 1965. Considering that seven papers are concerned with proteins one wonders why there is not a journal named Protein. Included in this group are three papers on protein structure and three on their binding properties. Eleven papers are on enzymes, specialized proteins that accelerate or inhibit biochemical reactions. Five papers describe the preparation and properties of a variety of enzymes. Two discuss enzyme kinetics and rate equations. TWO more papers discuss allostenc enzymes in bacterial metabolism. The emphasis on methodology is reflected in the large number of papers on electrophoresis, chromatography, centrifugation, and other techniques for separating large molecules. There are 16 papers on electrophoresis alone! The papers by Davis and Omstein on disc 258 bbchemical substances in tissue or fluids. Three papers d~uss various aspects of human and animal hemogl~ bin. One paper details the electron transport system in the outer membrane of liver mitt ~hondria. Other areas dealt with include the incorporation of radb active amino acids into proterns, the determination of cystine as cysteic acid, that and a scintillation machine measures the amount of radioactive materiaf in blologictd fluids. In the near future I will provide an additional list of life science papers of the 1%0s. These will cover all aspects of biomedical research except biochemistry. Following that I hope to cover clinical papers. I’m sure you can understand the frustration I experience in having to cut these MS off at an arbitrary point, knowing there are many additional important papers that should be listed. Science is such big business these days that even a listing of 1,000 papers would leave out many key people. So there must be an arbitrary cut-off point. Current Contents can’t provide unlimited space for this information. That is why I look forward to our Atlas of Science. 13 In it we expect to identify almost every signf]cant paper for each field and period studied. Since it has been four years since I first mentioned this project I should add that we hope to complete that project during the next year. ems Ial REFERENCES 1. 2. 3. 4. 5, 6. 7, 8. 9. Gatffakt E. Most-cited articles of the 1960s. 1. Physical sciences. Currem Contents (21):S-IS. 21 May 1979. Science Cit.fion Index 1978 Guide. Philadelphk: 1S1Press, 1979. 150p. Gnsflafd E. Trends in bkrchemical literature. Trend$ Biochem. .$ci. (In press. 1979). Barsky L Telephone communication. 7 June 1979. Kapfan N O. Telephone communication. 16 May 1979. Ifrenner S. Telephone communication. 16 May 1979. Watqon J D & Crfck F H C. A structure for deoxyribose nucleic acid. Namra 171:737-8, 1953. Garffekt E. Highly cited articles. 35. Biochemistry papers published in the 194%. Current Contents (8):5-1 1, 21 February 1977. Garfkfd E & StsarI. New tds for improving and evaluating the effectiveness of research. (Yovits M C. Gilford D M, WIICOX R H, Stavely E & Lemer H D, eds.) Research prwgmm ef~ecfiveness. Pmreed. mgs of the conference sponsored by Office of Na val Research. New York: Gordon & Breach, 1966. Chapter 7. p. 135-46. Washing/on, DC, July 27-29, 1%5. 10. Garlfefd E. Highly cited articles. 37. Biomedical articles pubfished in the 1940s. Currenf Cwrferm (13):5-12. 28 March 1977. II. Zssckermrm H. Scientific eltte. Nobel laureates in the United State.r New York: Free Press. 1977. 335p. 12. G2Uaqde D. Cmrfion Classics A quantitative assay for DNA-RNA hybrids with DNA immobilimd on a membrane. Current Conterm [11): 14, 14 March 1977. 13. Garfiefd E. lSf “sAt/as of Science may help sfudents in choice of career in science. Curwnr flmrmnls (29):S-11. 21 July 1975.(Reprinted in: Garffald E. E.way.rtI/ an informaoon .wienml Philadelphia: 1S1Press. 1977. Vol. 2. p. 311-2. ) F@lm ~: !wn. 10t mml.cllco ff m amcle amc!es of [he 1960s in biochemistry has appeared as a CtmmwI Clasm-. and molecular a reference biology. follows the amhor Authors’ affiliations follow each cita affiliations, Total Clmtforss 1%1-197s Bfblfogsapbk Data NUCLEIC ACIDS (DNA/RNA) I(YJS AmesB N J fho/ Ml Btltten 4 LSubfn D T. The role d pofyamines 235: M19-75. 19b0. NIH, Chem R Ii ~ osvfdms E Hz. Gene I I I Carnegie inst. of Washington. 121Rockefeller 1441 llnw., Erf[tea R f & Kohne Washington, DcpI New York, regulatmn DepI NY m the newralizatimr NfAMDD. Ten Srtbesda, Magnet of bacteriophage for higher celfs: a theory. .bence Magne!.. DNA. 20014 I bS:349-57. 1969 Washi”gf on, DC 20015 llH321 D E. Repeated sequences in DNA, TcrI MD W ashmgmn. 259 Screnu DC 20315 16 I: 529-Kf, l%t!. Carmgic Imt of 142 _ 920 CkQszLmfin RR. A Qm~h~ J. L601. Chem. 244:61607. M ● Lfers ?. DNAd#recwd PtKIC. Nal ,4cad Slmford, 71KI J%& f.r the iWEe =de Ptilcxlio. of E c.h DNA-dc~ndcnl 1%9. Harvard Llniv.. Biol. Lab., Cambndgc, MA 02138 syn[hews of RNA .$./. LJS 4L3:81-94, 1962 S!anford by an emyme ~Jmv Sch Med 1513 polym.rasc ../, Bmchc,n CA 90J5 A k Mmra H N. The precision of ullmviolct absorptm. measurements t. lhc Schrn#dt- Tfmnnfmu$cr procedure for nuclelc .ctd cstimstson. Bmchtm hi” GJassow, J3CJX Btahcm. Glasgow Scotland 724 from t DepI RNA Bmphy. A cIo 55 5’?I -83. 1962 Gfkae K W k Myers A. An Improved diphenyJamine rnelhod for !he esxim.oon d DNA Nmwv M93, 1%5. Uni*. Southampton. Dcp! Bmrmy, Southampton, England GEkpfc D G Sp@&! S. A quantttmve membrane. 1 Mol LJIoI 12 82%42, iCit*tiott Clusis>. C., ,=,;: 1%5 assay for DNA-RNA hybrids wl!h J)NA wnmobdw.td o“ a Univ. Illimm, Dept. !4 ?-!,,+ !Q~~ ! Microbml (Irban.. IL bll!Ol c.=::..:. !!!! !4, 753 JJkt 611 Hdfey B. SeJective extraction J. Mo{ fhol StmcIurc bb., 713 H- Mm Acad J, F@k Na[ 2433 Btol Lyon 1%1. Inst Marmur N~ Ctr., [Inn.. Denver. BdfofJ RNA J Sk& Zmmfr A. Sod md Nwr 148S3 symhcws f),, Bml Pmadcna. CA 9J 125 1’478 ] role of DNA by actinomycm m RNA sytuhms 3 rhc mhlbmor, D and pro flamn U.,, mccfunisms Sch cd Mcd DepI Mwrobwl,. Uno. Mol. Radiobiol. for the isol,tion Chem.. Biol., M W & ~ Befhesda. MD L60f Unit, or DNA c~.wr’Js HMwell, composition 1962. Harvard L DNA: Pm., US 57 151+21, SC, England and [1.,, mus.ulw L ) En@d of DNA [JIMV., Dept. J M./ of cell-lree Pro< the closed cwcufar DNA 1967 3:2(W 18, 196 I Bm/ from o% thermal denatmatmn Chcm., Cambridge, and protein symhcm.$ Scten.e Cafif. pro!ein N.f in 02 13ff S., cd, upon US 47. I WUJ2. 19bl detection and wlawm of HeLa cells Tcchnol., Inst. MA 145 13$%401. 1%4. synthesi$ m k A cad method for tbe A dyc-b.oyant+ermly cfoscd circular duplcl NaI, A cad Cambndgc, 02 13S I H. T6c dependence W & %’- R. - and acndmcs Cambndgc, from m,crworgamsms MA of the buc 5 10).18, P. RNA 2CO14 M W & Mnftkd of DNA Univ. 01 the mouse I MUS Rcs Cambridge, P. Determination J Me/. in the synthesu ol protcms Paris, France in the interaction naturdfy occurring or synthetic Polyribo..ckotides N[H. Belhcsda, MD 200f4 749 Plant CO @1320S 1%1. MRC, Dep( J & D@ Nbeaba~ Agnc Jthaca, NY Tcchnol Insl, New York P=teur. 1%1. MRC .%w?6mr J. A procedure NIH. 1070 1%2 consideraoom 3. lfb30. 190:372-J, Iempcmlurc. ’951 and DNA J. Gcnettc rcfwlalo~ fded Harvnrd 1134 RNA M F. Gene action in the X-chromosome Nawm Y978 CalIf S*>tmr\md Men4Jf S H. Penswkk LJcpt Bwdtem., ( 12) 9, 20 March US 4& f222.30, 3. J18-56, Biol Colorado 736 SCI M, K7312 J.eimsm L S. Structural J Mol. 1%2 Conmnl$ synthesis of NY Jacob F k Moms! J Mol. 695 (Jmv., J 1. R4akway M & Afczm.m2et M. Tlu Acad New York, Rcs., Lmwmnc, a supp.-cssor of cbromc-wmml US 4S:121&22, C.menl of tbe emymatic Pmc Cancer J T. Marqa& acid. Scwmcc 147 1462-5. 1965 US DcpI J. HMone, SI-I Ch.!ics. from utfected mouse cell cdtwm SW)S Inst. for Exp DC 20250 and Cornell R C & Boxmr [Clution khrwfw 1%7 DNA Everett G A, NldbLw of a ribonucleic Wasfunglon, %OC 630 2b%5t.9, R W, AWarJ, of polyoma bb Chem. BIOI Pasadena, CA 91125 6B0 Bdck E. Fraekkfs R M, Sbfkh ●nimal ceffs and viruses. Proc New York, NY KJ021 1[17 SehMkxaMI Not C L, R4mmmr J & Day dcttsity in CSCL 1 Mo/ 7to A J ● Tamm Acad E L. Act]on of aconomycm SC-I US 49 12Jf4.45. P. J3ctermirmtm” Bto/. 4433-43, .%tfow R B k CamJrr W L. ‘flIc disappeamnce mccfunii. Proc N.r Acad S.,. of the base compuimm Hawud 1962. Univ., DcpI Um. of DNA Chcm., of thymme dkmem lrom US 51:226-31, D on Rockefeller 1962. [mm m b.wyant Cambndgc. DNA. MA 0213U an crr.r-comccnng 1964. Oak R!dge NM. Lab Bml. Di, Oak Ridge, TN 37f130 %4 Wnmm Pmr J R. Kqf P M & JIM NaI Scr [Cimfwn 678 Acrid Classics WeceZz?sF A. A mulliple ribasomd J963. MIT, US 49:122-9, C.n’ent O. Swahs!SE T & NuS H. Rbosomaf of the ermxume. Pit[sburgk, Nafurc swucturc m protein L3cpI Bml., Contents (41) 11, 10 October 197:405, f9h3. Umv. Cambndgc. syn!hc.is MA 02131J J977. I a~rrgatc engaged m protein synthcsm pmsbur~b Sch O( Mcd DCPI chamcmnution M,crobto l.. PA15260 PROTEINSImrcrului f 242 Cre&&f A M, M-m boxymelhyfaied 910 SX#k-rbSS.Spectroscopic B,oche.wsfry 1114 S & ScekmW H. T31c preparation proteins. J. Utof ~ 6 1948-S4. Chem. determination 19h7. NIH, Sch. Med. Rcs., Mdboume. of tryfuophan NIAMDD, P ● %SE G. A protein scqucnatcu and enzymattc hydrolyw. of reduced and S-car- 23& b22-7, 1963. Jkockcfeller UmW., New Ywk, E.r CJiII Endocn.cd. J Bmchrm Australia 260 NY and tyrosine m proteins. f3r., Bethesda, MD 1.JW91, 1%7. S! 20314 Vmcent”s 1C021 851 studieson thestructured fromstriatedmuscle.J. Mol. Biol 7:281-33S.1963.MRC, JYmsJ8yH E. Electron microeco~ Mturd syntheticproteinJffmems and d Mol. L-b. Bii.. Cambridge. Engfand b% D E. NemwkiyG 4 *D. Compari$c.n of expctimmlalbindingdataand tbeoretkcalmatfda in proteins containing subunits. Biochcmi$wy 5:365-85. 1966. Brookhm’eu Nat. Lab.. Upton. NY KmkJad 11973 and RockefefJer Univ., 1821 Omam T & Sao be 645 nprotein New York. NY purification. pigment d Chum. 239:2J’08. nature. J. Sfio/ T ● SaIo R. The carbon monoxide OmBm 1002 I R. The carbon monoxide-bindine and propxties, Univ.. binding pigment Bio/ Chcm J Ji.er micraomes. 1964. hka 1. Evidence Inst. Profein of liver microsomes, 239:2379-85, 1964. Osaka Univ.. for ils Rcs.. Osaka. Japan 2. Sdubifizatiom Inst. protein Rea.. Osaka, Japan ENZYMOLOGY 760 D, KapbnN O, Juvh L & ZwEf@E. Nature●nd Cabo R Scirnce 1116 136:%2-9. Cfd%nd W W. and rate equations. DcpI. lCttation 648 Bmhem., & Surgccms, Dept. d A ● Javkrdbf of E. coh. Biorhim. McCo# MicrobioJ.. 1. Purification Biophy$. Chem. J. Mol. 6:3136-29. 1%9. E, 239:291W17. Pe4sky 705 NY of two new chromogenic Univ., Columbm Univ. Wffkkmon Cambridge. An enzymic Med. the enzyme alkaline phcmphamw phospha Pase. Ctr.. MA function Dept. 02139 for erythrocuprein Bicwhent.. Dmham, (hemocuprein) NC 27706 proteins and cellufsr control systems. transitions: s plausible model. S. Tyrosine hydroxyfasc: 1964. NIH. NHI, the ini!id Itafy step in “orepinephrine Lsb, of Cfin. Biochem.. A & Rackc? E. Partial resolution and properties Rome, Bethesda, MD biosymhmis. 2CO14 of the enzymes cats fyzing oxidn- of soluble, dinitrophenol-stimulated adenmine Chem 235:3322-9, 1960. Pub. Health Res. Inst of NY, New York, [’nit. Johnson R=. Fdn.. Phifa., PA NY CSIRO, Dh Math. l@316 & Phys. 19N34 G N. Statistical estimations in enzyme kinetics. Biocbn Adelaide. sub- COIL of Physicians 10032 BioL Dept., dwmumse. Duke 1. Purification J BIo/ 1. N& Coil. H & Estabcmk R W. Spectral studies of drug interaction wilh hepatic Scfwmkmmn J B, R=? microsomal cywchrome. Mo/ Ph.wtrmcol, 3:1 I 3-23. 1%7. Univ. Pemtsylvania. Dcpt. Biophys. Btochem.. II-I Wisconsin. Inst. Pssteur. Paris. France and Istituto Regina Elens, Sk S, 08tu ti, e phosphorylation. mphosphatase. 1963. Univ. cnd propertie! 1%1. J P. On the nature d dlosteric 12:8S-1 18.1965. Chem. M dehydrogenases. 02154 Inst. Pasteur. Paris. France 1%3. J A C%wgenx Biol. J Bio/. New York. L Superoxide Nagmas T, Savbt M ● Udenfrknd Pa&s 95:271-8. I ? ● Iacob F. Allosteric Biol. 1, W~n J Mol. Biophy.. and characl erization 01 alk dine 244:6049-55, MA 11 July 1977.1 W. The preparmion 3L7:471W33.1%43. MIT. Ac& Mrntod J, -x Moeod 67:104-37, Acfa C. A Jine-structure genetic and chemical study d I SS 4 Ftbfovieb J Bto/ Biochem. of ktic Wdtham, 537C4J {28):8, N ● Cokes development Dept., reactions with two or more substrates or products. Btophys WI Classics. Cuwent Conmnts ErfangerB F. Kokowsky Gsren Bmchim Madison, strates of ttypsin. Arc+. -7 8 Biol. & Chem. The kinetics d enzyme-catalyzed menclature Agric., 1%2. Brandeis Univ., J 80:324-32, f%l. Stat., Austrafia ELE~ROPHORESLS 651 Bbbop D SS L, t3aybroek pcdyacrylamide “92 K-$41 Clrsmback B J. Disc electrophorcsis. NY A cad Duoker NY S,,. Lawell Biochem. Lund, bordf and Biophys., Malmo ffmchem. Wisconsin. Bmchem, 20150. 1%7. OmsIefa Davis, CA 1%4 L. Disc eleclrophoresis, Sinai Hosp., Bmchem Ceff Res. hb., weight determinations Biophys. NJA ID, Hemamf., cm Pcdyacrylamide Lab and Dept. 126 f 55-64 Jhophy~ Biochcm., Uni. 1967. Ltmd, Anal Malmo (J.iv. Bmchem L“”d, Hosp., lJ”iv weights of California, New York, arid theory NY f %S. m agarosz gel comai”ing Depl. Cli” Dept. A.. Cbcm Lmd, antihodks, Sweden ac]d on Pc.lyacrylamide-gcl Botany, Edt”b.rgh, NY ,4 cod Sci Scotland 121:321-49.1964 ILX329 scrylamidc 1%9 !035.S-61, Sweden tibotmclcic Edinburgh, 1, Backgro.”d 130:337-46, 1968 q5b16 Dept. Clin. Chern,, R. High rescdMio” Biophy$ Bmr-hem of high-molecular-wei~ht J. 102:251.1, Panykm S ● Ckdkfey Arch f L 61UOl 10 hwmwt serum proteins. Cefl Res. Lab. a“d Dept. estimation of prcmeim by electrophoresis 15.45-52, phoresis. Biochem. ,4 r<h crossed elecwophoresis Hosp U E. The fractiomtion Loedug MI. Ge”, C B. Quantitative Anal fu74 on molecular Iqhq. [Inli. clec!rophomsis, C B. Anligen-antibody Univ. 276S And kkedrick J L & Smhb A J. Size and charge isomer separation and estimation of molecular Ocpl. 159t Urbana. for rapid and sensitive s[ainmg of 53706 prolcins by disc @ I 337 R R. Obscr\atmm 244:5074-60 Citem. WI Sinai Hosp., of tiraf nucleic acids o“ Microb,ol., N3L29 A K 4 Raeckert Madison. J. A proccdwc and application 196.4 MI. separation Jlfinois, Dept. gel electtophormis, 2 Method 121404-27, 1967. U“ii. M k Zwxarf NYJt4 gel. J Bml. M8 WyckoN by polyacrylamide Dwb S. Eler.trophomtic 26:373-87, NJH, Bethesda, MD New York. “23 Rebfe!dR A. A, BIo/ protein fractionated A.. -Is J R 4 Spfegefutm gels. J. hfol Ilni, 261 gel electrophorcsis Iowa. Dept of histoncs, Biochem,, Jowa City, IA 52240 clcctrw 6fm A C ● %-C pea.?+ W. agarmeacrylamide Bethe$da. MD 1!434 TM&&d weight cs[imation and s.eparaoaon 01 RNA by elcctrophorcsts 7:668-74, IW. NIH,NCI,Chcrn. Eels. Bjochemi. fry A, hwb U J A W8Jkma D R acrylamide 784 Molecular campsite gels. A’afurR 195:281-3. E. Ihk cleclrophoresu 1%2. Merck. 01 bamc protein! Sharp & Dohme %-%er F. Bm=dee G G ~ B.mm2fB G. A two-dimensional radioactive nucleottdes. J. Mot Btol and pcphdes cm POIY. Rcs. Lab., Rahway. N] 07065 [rmtionanon procedure [or Lab of Mol. Biol Lhmbndgc. 13:373-95. 1965MRC, 2544 Sbspfro A L!, E~ A Maid J V3. Vkmda phoresis m SDS-polyacrylamide Lk!iv. Sch. of Med., Colt. Med., I lW Molecular Eels. Biochem (I) Dept Ophthalmol Dept. Cell BioL, V=za@crberU01 & Svem mturd weighl estimation of pulypcptide Btophys (2 I Dept. New York, NY Res M. The polyacrylamide Cambridge, 1967 New York KM! 6 (31 Albert reliability of molecular J #to/ EmMcm 10461 studies on the rrs,>l.wg gel clectropbores~. MA NY England ehams by clectrm Hz. Isoelectric Iractionat] on, analysts. and characterization pH gradtcnts. 4. Further WebcmK & Oak 28:815.20. Commun Rloche m., New York. pwcr my%?lObin~ A,/IY Chcm $cand. 2@82@34 1~ 11) No~l Sweden (2 I Chalmcn Inst. of Tecbnol.. DcpI Pbys. Chcm 9x4 m Br., ~14 i. connccuon weight determinations Chum of ampholytcs with sep.raucm Med. Imt.. Bmchcm DCPI Gothcnburg. Sweden I %9. 2444406-12, m of Stockholm. by dodccyl sulfak. Harvard [Jniv Biol. Lab., 0213.9 CHROMATOGRAPHY 1944 Adsews 278? .AAmws P. The gel-filtration J %:595-606, Bmch.m. P. Estimation Bfochem. 674 ~ J 91:222-33, J B, Nae@s~ twhaviour I %5. 1%4. Wt. Hb Chesapeake and Hb J (Bankok). Depts. Biophys. and Med., Csm~ ‘?51 Dfttsmar J C A Lea@r P, WR.&L Acwd. 773 ?ohzm E W. [Citation _mf F%z I :6&77, NY J Am. 633 Univ. 1964 Lab of Chem Kentucky Biul.. CoO. Med Dep! Univ. Carnegie 1960. 1%2. Uppscda. Uppsala, column iden(ific~tion. Rochester Sch Med mcxffied procedure verification Dept. Genet., Oil Chem. Soc 40:425-54, Bethesda Btophys Acts 112:346-62, Univ., DcpI MD Biocbem 2LY314 Lipid com~simm of molecular Univ. I W. Baltimore. Bmchem J, ‘W:374-7, of beef bra,.. MD [964. Tennessee, Wkbker Ioal Wh Anal. ZetI Univ. ( I I Cornell M & Wclk W W. I R. Determination Chem 35:19! 21iophys Nat. Taiwan Univ., T. Aria Med. GasAiiuid 19b7 chromatography So.. TN 37916 New 262 Rye. NY chroma- New York, 10.MO PA of trmwthykdy( 15261 1977 ] Food Sci York Taiwan Di\., 8S: 2497-5o7, I %3 Phtsburgh. of phosphdtpids Pharm., weights of proteins by gel filtration C?dif., Dept. Taipai, Chemothcr fnst. for Pharmaceut. Scpsratic.n of dansyl-amino IJ3:369-70. Knoxwlle, CoO., Sloan .Kettering chromatogmphy Munich, of molecular Dept. Chem., Chzm & Nuo-it.. Thin-layer 1%1. Univ. Bmchem., m crude 1978. ] 143k9, 24 October 03.1963. Univ K R & WaES K Brochim Dept. Biochem. L A WOWS P. 334:175-84, DepI CA 91010 ratxn of proteins m Application anafysjs of phosphcdipids by thin-layer InsI. for Cancer Res., Div. of ERP Classics. CzmrRm Co.mnfs H, J40&mr Biochem 1022 Sch. Med.. and lhe 21205 derivatives of sugars and related substances. J Am Pittsburgh beef liver of complex lipid mmtures. Cm. Dept. Biochem.. DuarIe, weights and fractional Contents (I): 12, 2 January Swaefey C C, RzQtfey U, Mak!ks lCkmion NY 1977.1 fractionation City cd Hope Mcd 1963. K L Determination I(Y32I (2 I Sloan-Kettering WaSrm? Cold Spring Harbor. for [he automatic analysis of amino acids NIDR, Con fent. (2JI: 10.6 Jun. [Citation Cfassks. Current 626 Lon&m. 1979 I and analysis of phospha!ides. two apprcracbes to quantitative and Johns Hopkins Univ. 2CO14 Sweden and Dent Skfpakl V P1, Peteswm R F2 ● !fam16y M2. Quanotative I 555 MD on thin-layer Bmchcm March impure systems by use 01 gel filtration and densily gradient cenwifugatmn. preparations of suUite and hydroxylaminc reductases. NY Bethesda. for analysis O( nucleic acids. Inst. of Wtuhington, $eparafion, Univ. 21( 1I 1:14.12 ScIem-es of gel filtration and its cxperimenml 1%. I: 187-201, 1960. NIH. Skgef L M & MOMY tography. .Sch Med., melhcds for histone fractions from calf thymus. KrftchevskyG, JJelbr D & Lkkr E. Btochim. Uni> by affinity chrom.w~raphy 14627 i3/och.m sea anemone: Johns Hopkins 1966. NIAMDD, ComenIs/Life J. A theoiy [Citation Cfas!ics. Cufrent Jfoemer G, 19:91-WS, md of IWO new variants, 21205 A D. A fractionating K A & McwrkL. A Anal 812 5:126-7, 14:317-W. 3: I -20. Rm Rochester, 758 Res. G V. Chromatographic J L/pld Sep.rahon and the determination A simple, specific spray for the detection of phcspholipids Classics. Current J D & JSemkey Anal Bmchem 11724 638 England 1964. IIIM. Cancer Rcs., Chester Beatty Res. Inst.. Royal Cancer Hosp.. J Chmmmography Mam3zU Bio/ MD Berkshire. 1968 NIH. T C ● KCh!dzr k.amm Shinfiekf, US 61:636-43, J. Ltptd wide range. 40KJ7 J 92:55-9. England 1478 J. Mol. Baltimore, Studies on histories. 7. preparative 3fiochem 702 KY ● England human hemoglobins. C B. Selccli.e enzyme purification R L. weights over Berkshiw, M ● Aafk+n Srt. chromatogmms. Lexington. Res. Dairying, Inst. of (he e and /3 chains by chromatography. 710 No/. Shinfield, weights of ptotcins by sephadex gel-filtrrdion. M A & Wea?!smaff D J. Abnormal chamcterimtion Proc- of proteins related to [heir molecular Nat, Inst. Rcs. Dairying. of the molecular @+ Tech.. Dmis, acids by polyamide Blood CIr.. and glycofipids M.nicb. FRG on sep!iadel. CA ‘+W16 layer chromatqraphy. New York. NY 1002 I and CENITUFUGATION/SEDJiWENTAllON 799 &wea R J & Ra If 2S. W)gh-msolution SCW.CC 131:32-3, 1960, Camegic m Harbor. 3WS D. Sedimentation btuJ E 4 Jfeubcy A lhophy, J. 3XF)-21. NY F W. adysis. Magnet.. d molec.fsr 1.s1. of Washingtcm. B N. A method for dctermtitng otein mlxnwes. J. BIoI. 1762 Stn$!fer 2332 Ypkmwfs 0 A. Equilibrium Sedimentation Univ.. Stanbrd rale as a mess.m 1963. Camegte sedimentation Dept. Tar. Gcnet. Washington. DC 20005 weigh! of DNA. Rcs. Unit. Cokd Spring I !724 R G & Ara= Mardn 10, densily gladicnt IIISI. of Washm@on, Rockefeller Chem Dcp!. New York. NY d J. Mo(. Biol apphcatiom enzymes: Bethesda, 20314 MD 11:373-90. 1%5 Pa!n Alto. CA 94W5 B!ochcm.. alraccntrifugation behavior NIAMDD. studies C4 the size and shape of DNA. Sch. Med.. Univ.. the sedimentation 1961. NIH. 231x1372-9. of dilute solutions. Biochemistry 1964. 3’297-317. ICQ21 MISCELLANEOUS 1014 AdzfSxrg E A, Mmm46f SS & C&n N-nttwN-”itm~uanadtne Yale Unit., D+. woods Hofc. MA 9W MicrobioL, 02S43 Methods for Arafitoff D. New Yurk, lhe quantitatiw P J. NcuropathoL. Icitation %=h C’kmcs. IU12 Univ., mclhork 10 ?41-53. Current Ncw York. Con!ents NY of hemoglobin. b5S M. A modified Med. Uni!. Anal. Biochevn o\- Arch. Lab., Charloucsville. VA Cfaksxd W W. DepI. Commun. 26:162-7, pamrosanihn Div. 00 Ihc 1%7. New York. Area/. B/ochem NY 1C1332 4:33b-4. 1%2 aqueous solutions in a liquid scmtilla!icm NIH, NHI. Lab. Kidney & Electrolyte f2t 2’. 10 lammry 121 96-102. Metab., MD Bethesda, 1977. I cm the oxygen equilibrium Unn 1%7. Virgm]a Sch of Med c1 Biocbcm 22903 a new pro[ecti$ c reagcm for SH groups Biochem., Madison. WI Res. Lab I SS2. A simple me!hod of long-chain Bcckcnham, 34802. 1964 1%4 fatty acids. Kent. for the preparalton J W14--9 Baochemu:r,v 531Jb mwrmdctcrmmauon E“gfand of 32 P-fabdcd Camhridgc, Unm. adcnomw { 11 Phywol Lab mph(nphatc 12) f)rpl Cam brtdg=, England N E. WfngeI D. Wfmter W, Comioffy research. Bmchemtsx,? lo~scal Res. for coun!mg Bmph.v f963. Wcllcome & Ckp@?ff Bmchcm., using hexaonium HcE+. of New York, Sinai Dept. of Bioc6em., J fW~-fO. Chod 10 lnc.. 1978.1 Bmphys CkIIrIComdMW G. The colwimetric I MI M(. of orgamc and inorganic pbosphams B!ochem Dlthiothreitol. Wis.xmsin. Gfyrm of New York England 19MI. of high specdic activity. Biochem <w) 1%2. uronic acid carhazole reaction. London, A & Ctmt+?fi R R. Effccl Jfmchcm llb5 acid and their applicatmn Health Res. lint. for acid phospbamse Btochem 1:27’3-85, human ery!hrocytcs. [l.,, 1965. Biol. Lab.. lC4f29 of Physicians & Surgeons, Bray G A. A simple efficient liquid scintdlator *mIdn 1%1. Publ. llf):~. 20 February 203!4 lCitation Classics, Currenf C..te.I.< bl I 18:78S-9S. Hole hfarinc R E. The effect of orgamc phrmphates from fhc human erylhrocyle Gil. SkNer T & Mdr H St Mary’s HOW., c,m.tm. Re% Commun. (of N-acetylneumminic J. 81:384-92, Cy(ocJiem Pathol., properfics Columbia 15& Dept. R & WmzdI alkteric estimation Biochem for mutagenesis hy N-mcthyl- Bmphys CT 06S20 and Woods Histochemical u coupler. /. Jfistochern. b.yl condhioos NY NW6 T ● A-m Rsrka optimal New Haven, hydrolysates of sialomucoids. 925 G CC. in E. cola K 12. Bmchem. T N, Imwt l%b 5467-7- S & Michigan Sfngh R M M. State tlm% Hydrogen Dept ion buflcm (or tnu Botany & Plant Pa!h<,l Eaw Lansing, MI 4fJf123 llt13 Hahomorf S. A rapid permethylation mn m dimethyl ?.ulfonide. J of glycolipad. and pofysaccbande Cancer Res.. Odawam-Nankozawa, b“4 Kunovsky J I 22s M J & Rum Hirbc/Iem. MSM Db Moore dsk Morrkm New York, NY B1oI.. HiIfs Road. And Med 944-53, Lhoph V, Sch Oept. of radioactive Pathol.. amim Bostcm. MA 0?1 15 h> a La b.. Stof. of cystinc as cysteic mcid J BIOI Chem 23S235 -7, 1%3. Rockefeller 10021 cd 1.UY acid methyl esters and dimethylacelals J Ltpd ReJ 5:W8. 1964 Unw. Calif. DepL H, ox J M & Goamau 2.fJ~resolwo”: Cambridge, from Fcad Sci. L C G. Tbrcedimensional the atomic mode!. Fourier 14amre 219:131-9, 1%8 D J ● Udc6ftfemd S. A specific method for Ihc analysis of hydroxyprolinc ffiochem 1.22ki-39, f9h0. NIH. NHI. Exp. Thcr. & Lab. Cbn. Bmchem W—r Stockholm, MRC, Lab.hfdec. Wermer-Gren fml., Stockholm, Sweden and Karolin.*a in Iiwucs nnd urine. Brthesdz, 629 S!ockholm. synthesis of horse England A. An electron-lransfmrt %tioasa G U Kmykm!kma Jf, Ernmer L ● Bergstnnd wjth the ouwr membrane of liver rnimchondna. J Cell Bml .32:4f $38. 1967 Insl MD 20314 sy$tcm msocialed Ocpl Palhol. II, Sweden I F. TfK determination d tions of this amino acki. Arch !nsl., Inw acids mm protcm 1961 Oak R!dgc Nat 6h- Uni. Sch Davis. CA 9561b Perotz M F. S4aSr&zd Frockop Uni.. of the mcorfmration Biocht’m fluoride-methanol. o,yhaemoglobintt -11 Pharmaceut. thkochofine methcd for chohneswrascs. 1’464. Harvard W R ● %aftb L M. Preparation .S Tech., catalym?d by mc(hylsulfmy I cdrban - Tohoku TN 378Xf S. On the determination lipids wiih boron 582 12219-21, method. .4rch. Oak Ridge. llni}.. 819 L. A “d!rect.colonng”’ Cjmchem. 55 205-8. 1%.. Scndai. Japan Sf J & Nbvefff G D. Measurement filfcr-paper ] 52. — Tot?. B,ochem Lab. Biochem.. Miami, hydroxypro fine in tissue and protcm samples containing Bio.-hcm fl 331W. Btophyj. 93440-7. and Univ. Mimm, 263 1961. Howard Dcpt, Biochem small propor Hughes Mcd Mtmni. FL 3.1136