Methods in Enzymology

Total Page:16

File Type:pdf, Size:1020Kb

Methods in Enzymology METHODS IN ENZYMOLOGY SIDNEY P. COLOWICK NATHAN O . KAPLAN VOLUME I PREFACE V CONTRIBUTORS TO VOLUME I X i OUTLINE OF ORGANIZATION, VOLUME I xV OUTLINE OF VOLUMES II-IV xxi i Section I. General Preparative Procedure s 1. Tissue Slice Technique K. A. C. ELLIOTT 3 2. Tissue Homogenates VAN R. POTTER 10 3. Fractionation of Cell Components of Anima l Tissues GEORGE H . HOGEBOOM 16 4. Preparation of Mitochondria from Plants BERNARD AXELROD 19 5. Preparation of Chloroplasts and Disinte- grated Chloroplasts PAUL R. GORHAM 22 6. Methods of Extraction of Enzymes from Animal Tissues ROBERT K. MORTON 25 7. Extraction of Enzymes from Microorgan- isms (Bacteria and Yeast) I. C. GuNsALUS 51 8. Extraction of Soluble Enzymes from Higher Plants ALVIN NASON 62 9. Disintegration of Bacteria and Small Par- C. S. FRENCH and 64 titles by High-Pressure Extrusion H. W. MILNE R 10. Protein Fractionation on the Basis of Solu- ARDA ALDEN GREEN and 67 bility in Aqueous Solutions of Salts and WALTER L. HUGHE S Organic Solvents 11. Separation of Proteins by Use of Adsorbents SIDNEY P. COLOWICK 90 12. The Partition Chromatography of Enzymes R. R. PORTER 98 13. Chromatography of Enzymes on Ion Ex- change Resins C. H. W. HIRs 113 14. Special Techniques for Bacterial Enzymes . Enrichment Culture and Adaptive En - zymes OSAMU HAYAISHI 126 15. Separation of Proteins from Nucleic Acids LEON HEPPEL 137 16. Preparation of Buffers for Use in Enzym e Studies G, GOMORI 138 Section II. Enzymes of Carbohydrate Metabolism 17. Amylases, a and ß PETER BERNFELD 14 9 18. Pectic Enzymes Z. I. KERTESZ 15 8 19. Mucopolysaccharidases ALBERT DORFMAN 16 6 20. Cellulase Preparation from Helix pomatia (Snails) GEORGE DE STEVENS 173 21 . Polysaccharide Synthesis from Disaccha- rides EDWARD J. HEHRE 178 22. Phosphorylases from Plants W. J. WHELAN 192 23 . Muscle Phosphorylase GERTY T. Cora, 200 BARBARA ILLINGWORTH, and PATRICIA J. KELLER 24. The PR Enzyme of Muscle PATRICIA J. KELLER and 206 GERTY T. Corn 25. Amylo-1,6-glucosidase GERTY T. Cora 21 1 26. Polysaccharide Phosphorylase, Liver EARL W. SUTHERLAND 21 5 27. Branching Enzyme from Liver JOSEPH LARNER 222 28. Disaccharide Phosphorylases M . DOUDOROFF 225 29 . Hexoside Hydrolases SHLOMO HESTRIN, 23 1 DAVID S. FEINGOLD , and MICHAEL SCHRAMM 30 . Methods for Measuring Transglycosylase Activity of Invertases J. S. D. BACON 258 31. Glucuronidases WILLIAM H. FISHMAN and 262 PETER BERNFELD 32. Yeast Hexokinase MARGARET R. MCDONALD 269 33 . Animal Tissue Hexokinases ROBERT K. CRANE and 277 ALBERTO SOLE 34. Fructokinase (Ketohexokinase) H. G. HERS 286 35 . Galactokinase and Galactowaldenase LUIS F. LELOIR and 29 0 RAfm E . TRUCC o 36. Phosphoglucomutase from Muscle VICTOR A . NAJJAR 29 4 37. Phosphohexoisomerases from Muscle MILTON W . SLEIN 29 9 38 . Phosphohexokinase KUO-HUANG LING, 30 6 WILLIAM L. BYRNE, and HENRY A. LARDY 39. Aldolase from Muscle JOHN FULLER TAYLOR 31 0 40. Aldolase from Yeast WALTER CHRISTIAN 31 5 41 . Fructose-l-Phosphate Aldolase from Liver FRANZ LEUTHARDT and 320 H. P. WoLF 42a. Glucose-6-phosphate Dehydrogenase A. KORNBERG and 32 3 B . L. HORECKE R b. 6-Phosphogluconic Dehydrogenase B . L. HORECKER and 323 P. Z . SMYRNIOTIS 43 . Glucose-6-phosphate and 6-phosphogluconi c Dehydrogenases from Leuconostoc mesen- teroides R. D. DEMoss 328 44. Glucose Dehydrogenase from Liver HAROLD J. STRECKER 33 5 45. Glucose Aerodehydrogenase (Glucose Oxi- dase) RONALD BENTLEY 34 0 46. Hexose Phosphate and Hexose Reductase JOHN B. WOLFF and 34 6 NATHAN O. KAPLAN 47. Gluconokinase SEYMOUR S. COHEN 35 0 48. Synthesis of Glucose-1,6-diphosphate Luis F. LELOIR and 35 4 RAfiL E . TRUCCo 49. Yeast Pentokinase HENRY Z. SABLE 357 50. Phosphoribomutase from Muscle HANS KLENOW 36 1 51. Pentose Phosphate Isomerase BERNARD AXELROD 363 52. Pentose Isomerases SEYMOUR S. COHEN 366 53. Transketolase from Liver and Spinach B . L. HORECKER and 371 P. Z . SMYRNIOTIS 54. Crystalline Transketolase from Baker's G . DE LA HABA and 375 Yeast E . RACKER 55. Transaldolase B. L. HORECKER and 381 P. Z . SMYRNIOTIS 56 . Deoxyribose Phosphate Aldolase (DR- Aldolase) E. RACKER 384 57 . Triosephosphate Isomerase from Calf Muscle GERWIN BEISENHERZ 38 7 58. a-Glycerophosphate Dehydrogenase from GERWIN BEISENHERZ, 39 1 Rabbit Muscle THEODOR BLUCHER, and KARL-HEINZ GARBADE 59. Glycerol Dehydrogenase from Aerobactor aerogenes ROBERT MAIN BURTON 397 60 . Glyceraldehyde-3-phosphate Dehydrogen - ase from Muscle SIDNEY F . VELICK 401 61 . Glyceraldehyde-3-phosphate Dehydrogen - ase from Yeast EDWIN G . KREBS 407 62 . TPN Triosephosphate Dehydrogenase from Plant Tissue MARTIN GIBBS 411 63 . Phosphoglycerate Kinase from Brewer' s Yeast THEODOR BtICHER 415 64. Phosphoglyceric Acid Mutases PETER OESPER 423 65. Enolase from Brewer's Yeast THEODOR B$CHER 427 66 . Pyruvate Kinase from Muscle THEODOR BiicHER and 435 G. PFLEIDERER 67. Lactic Dehydrogenase of Muscle ARTHUR KORNBERG 441 68. Lactic Dehydrogenase from Yeast MALCOLM DIXON 444 69. Lactic Dehydrogenase of Heart Muscle J. B . NEILANDS 449 70. Glyoxalases E . RACKER 454 71. Plant Carboxylases THOMAS P. SINGER 460 72. Acetoin Formation in Bacteria ELLIOT JUNI 471 73 . Phosphoroclastic Split of Pyruvate, Yieldin g Formate (E. soli) HAROLD J. STRECKER 476 74 . Phosphoroclastic Split of Pyruvate, Yieldin g Hydrogen (Clostridium butylicum) H. J. KoEPSELL 479 75. Phosphate-Linked Pyruvic Acid Oxidase L. P. HAGER and 482 from Lactobacillus delbrückii FRITZ LIPMANN 76 . Coenzyme A-Linked Pyruvic Oxidase (Ani - mal) S. KORKES 486 77 . Coenzyme A-Linked Pyruvic Oxidase (Bac- terial) S. KORKES 490 78 . Liver Alcohol Dehydrogenase ROGER BONNICHSEN and 495 NORMAN G. BRIN K 79. Alcohol Dehydrogenase from Baker's Yeast E . RACKER 500 80. TPN-Alcohol Dehydrogenase from Leuco- nostoc mesenteroides R. D . DEMoss 504 81 . Potassium-Activated Yeast Aldehyde De- hydrogenase SIMON BLACK 508 82. TPN-Linked Aldehyde Dehydrogenase from Yeast J. EDWIN SEEGMILLER 511 83. Liver Aldehyde Dehydrogenase E. RACKER 51 4 84. Aldehyde . Dehydrogenase from Clostridium E. R . STADTMAN and 51 8 kluyveri ROBERT M . BURTON 85. Flavin-Linked Aldehyde Oxidase HENRY R . MAHLER 523 86. Glycolic Acid Oxidase and Glyoxylic Acid Reductase ISRAEL ZELITCH 528 87. Formic Dehydrogenase from Peas ALVIN NASON and 536 HENRY N. LITTL E 88. Formic Hydrogenlyase from Escherichia coli MAX BOVARNICK 539 Section III. Enzymes of Lipid Metabolism 89. Fatty Acid Oxidation in Mitochondria ALBERT L. LEHNINGER 545 90. Fatty Acid Oxidation in Higher Plants P . K. STUMPF 549 91. Butyrate Enzymes of Clostridium kluyveri H. A. BARKER 551 92. Butyryl Coenzyme A Dehydrogenase HENRY R. MAHLER 553 93. Crystalline Crotonase from Ox Liver JOSEPH R . STERN 559 94. ß-Ketoreductase FEODOR LYNEN and 566 OTTO WIELAND 95. Enzymes of Acetoacetate Formation and Breakdown JOSEPH R. STERN 573 96. Aceto-CoA-Kinase MARY ELLEN JONES and 585 FRITZ LIPMAN N 97. Acetate Kinase of Bacteria (Acetokinase) IRwIN A. RosE 59 1 98. Phosphotransacetylase from Clostridium kluyveri E. R . STADTMAN 596 99. Coenzyme A Transphorase from Clostridium H. A . BARKER, 599 kluyveri E. R. STADTMAN, and ARTHUR KORNBERG 100. Deacylases (Thiol Esterase) JOHN GERGELY 602 101. Acetylation of Amines with Pigeon Liver Enzyme HERBERT TABOR 608 102. Acetylation of D-Glucosamine by Pigeo n Liver Extracts MORRIS SOODAK 61 2 103. Amino Acid Acetylase of Clostridium kluy- I. LIEBERMAN and 61 6 veri H. A . BARKE R 104. Choline Acetylase DAVID NACHMANSOHN and 61 9 IRWIN B . WILSON 105. Acetoacetate Decarboxylase H. W. SEELEY 624 106. Lipases M . BIER 627 107. Acetylcholinesterase DAVID NACHMANSOHN and 642 IRWIN B . WILSON 108. Dialkylphosphofluoridase A. MAZUR 65 1 109. Liver Esterase ELMER STOTZ 657 110. Phospholipases OSAMU HAYAISHI 660 111. Enzymatic Phospholipid Synthesis : Phos- phatidic Acid ARTHUR KORNBERG 67 3 112. Choline Oxidase J. H. QUASTEL 67 4 113. Cholesterol Dehydrogenase from a Myco- bacterium THRESSA C . STADTMAN 67 8 Section IV. Enzymes of Citric Acid Cycl e 114. Crystalline Condensing Enzyme from Pig Heart SEVERO OCHOA 685 115. Aconitase from Pig Heart Muscle CHRISTIAN B . ANFINSEN, JR . 695 116. Isocitric Dehydrogenase System (TPN ) from Pig Heart SEVERO OCHOA 69 9 117. Isocitric Dehydrogenase of Yeast (TPN) ARTHUR KORNBERG 70 5 118. Isocitric Dehydrogenase of Yeast (DPN) ARTHUR KORNBERG 707 119. Diphosphopyridine Nucleotide Isocitric De- G. W. E. PLAUT and 71 0 hydrogenase from Animal Tissues S.-C. SUN G 120. a-Ketoglutaric Dehydrogenase System and Phosphorylating Enzyme from Hear t Muscle SEYMOUR KAUFMAN 714 121. Succinic Dehydrogenase WALTER D. BONNER, JR . 72 2 122. Fumarase VINCENT MASSEY 72 9 123. Malic Dehydrogenase from Pig Heart SEVERO OCHOA 73 5 124. "Malic" Enzyme SEVERO OCHOA 739 125. Oxalacetic Carboxylase of Micrococcus lyso- deikticus DENIS HERBERT 75 3 126. Oxalacetate Synthesizing Enzyme MERTON F. UTTER and 75 8 KIYOSHI KURAHASH I AUTHOR INDEX 765 SUBJECT INDEX 785.
Recommended publications
  • Independent Discovery in Biology: Investigating Styles of Scientific Research
    Medical History, 1993, 37: 432-441. INDEPENDENT DISCOVERY IN BIOLOGY: INVESTIGATING STYLES OF SCIENTIFIC RESEARCH by NICHOLAS RUSSELL * INTRODUCTION The fact that discoveries are often made independently is a commonplace of the history and sociology of science. Analysis of independent discovery has potential for evaluating the relative importance of social and individual components in the conduct of scientific research.' For instance, in a classic paper, Barber and Fox2 discussed the independent discovery of a bizarre phenomenon by two scientists. Aaron Kellner and Lewis Thomas both found that injections of the enzyme papain caused the upright ears of rabbits to droop over their heads like spaniels'. At first neither could find an explanation for it. Both abandoned the search and Kellner never returned to it, even though he went on to use the floppy ear response as a technical assay for measuring the potency of papain samples. Lewis Thomas did look into it again and discovered that papain completely altered the structure of the matrix of cartilage, not only in the ears but everywhere else in the animal as well. Both Thomas and Kellner had originally missed these changes because they had assumed that cartilage was a stable and uninteresting tissue. Barber and Fox concluded that Thomas persisted with the problem because it played a role in his developing research while the floppy-eared phenomenon was irrelevant to Kellner's interests. Barber and Fox hinted that more personal factors were involved as well, a theme expanded by Thomas in a later autobiographical essay.3 Thomas had found the collapsed ears amusing.
    [Show full text]
  • The Story of César Milstein and Monoclonal Antibodies: Introduction Page 1 of 4
    The Story of César Milstein and Monoclonal Antibodies: Introduction Page 1 of 4 Custom Search Search A HEALTHCARE REVOLUTION IN THE MAKING The Story of César Milstein and Monoclonal Antibodies Collated and written by Dr Lara Marks Today six out of ten of the best selling drugs in the world are monoclonal antibody therapeutics. One of these, Humira®, which is a treatment for rheumatoid arthritis and other autoimmune conditions, was listed as the top selling drug across the globe in 2012 with a revenue of US$9.3 billion. Based on its current performance many predict the annual sales of the drug will surpass the peak sales of Lipitor, a treatment for lowering cholesterol, that is the best selling therapeutic of all time. Currently monoclonal antibody drugs make up a third of all new medicines introduced worldwide. http://www.whatisbiotechnology.org/exhibitions/milstein 4/13/2017 PFIZER EX. 1524 Page 1 The Story of César Milstein and Monoclonal Antibodies: Introduction Page 2 of 4 Portrait of César Milstein. Photo credit: Godfrey Argent Studio Monoclonal antibodies are not only successful drugs, but are powerful tools for a wide range of medical applications. On the research front they are essential probes for determining the pathological pathway and cause of diseases like cancer and autoimmune and neurological disorders. They are also used for typing blood and tissue, a process that is vital to blood transfusion and organ transplants. In addition, monoclonal antibodies are critical components in diagnostics, having increased the speed and accuracy of tests. Today the antibodies are used for the detection of multiple conditions, ranging from pregnancy and heart attacks, to pandemic flu, AIDS and diseases like anthrax and smallpox released by biological weapons.
    [Show full text]
  • Eulogy Professor Emeritus Brigitte A. Askonas You Have Doubtless Often
    Eulogy Professor Emeritus Brigitte A. Askonas You have doubtless often heard it said that such a person needs no introduction. Well, I reckon the recipient of the 2007 Robert Koch Gold Medal deserves an introduction. I would like to introduce her, as she is not someone to blow her own trumpet. She would never describe herself as the grand dame of cellular immunology. She would never talk about the great influence she has had on immunology. She would never say that she has mentored countless outstanding scientists. She would never proudly list all her honorary memberships of scientific societies and academies and all her honorary professorships at top universities. Professor Brigitte Askonas is not very forthcoming about her successes, which is precisely why an introduction is necessary. We would like her to know how much we value her contributions to science and how impressed we are by the formative influence she has had on the biosciences in Europe and in particular on immunology. Ita Askonas started her scientific career as a biochemist. In 1944, she was awarded a bachelor’s degree in biochemistry from McGill University in Montreal, Canada. In 1952, she received her PhD from the Biochemistry Department of the University of Cambridge in the United Kingdom, where she served her scientific apprenticeship under Malcolm Dixon. She studied muscle enzymes, by no means the worst grounding for her subsequent research. After completing her doctorate, she became a member of the Scientific Staff at the National Institute of Medical Research in Mill Hill, London. There, she first continued with her enzyme studies and biochemical research.
    [Show full text]
  • NATURE July 12, 1947 Vol
    44 NATURE July 12, 1947 Vol. 160 The energy, enterprise and judgment he displayed build up the new Russia on sound and progressive during the difficult war years would be considered lines. exceptional, even in one trained to important Stalin succeeded Lenin and, under his leadership, administrative tasks. That they should be found in the Soviet Government gradually assumed its present a man of science brought up in academic seclusion form. The State Political Administration, afterwards and long confined to the narrow paths of fundamental the G.P.U., was created in 1922, and rapidly grew to scientific research may be thought a portent. be a powerful instrument of Government policy. On this subject, the memoirs are singularly Ipatieff's position became increasingly dangerous. revealing and present an interesting psychological His refusal to join the Party, his outspoken. criticism study. Perhaps the main characteristics of the author of his political colleagues and his frequent visits may be summarized as an abiding enthusiasm for abroad served to arouse the suspicion of the G.P.U. scientjfic studies, a deep sincerity of purpose and Many of his contemporaries were arrested and abounding self-confidence. From that day in early imprisoned or executed. "I reckoned," he says, youth when, with some trepidation, he waited upon "that up to 1930, of all the military engineer-techno­ the great chemist Mendeleeff and received from the logists who had completed their training at the lips of the sage an opinion that his knowledge was Artillery Academy, only two or three were left in too meagre for experimental work, until the occasion Soviet territory.
    [Show full text]
  • DAVID Green’S Death in 1983, Frank a Huennekens, One of Green’S Postdoctoral Fellows, Wrote in His Personal Recollections
    NATIONAL ACADEMY OF SCIENCES DAVID EZRA GREEN 1910–1983 A Biographical Memoir by HELMUT BEINERT, PAUL K. STUMPF, AND SALIH J. WAKIL Any opinions expressed in this memoir are those of the authors and do not necessarily reflect the views of the National Academy of Sciences. Biographical Memoirs, VOLUME 84 PUBLISHED 2003 BY THE NATIONAL ACADEMIES PRESS WASHINGTON, D.C. Courtesy of the University of Wisconsin Department of Photography, Madison DAVID EZRA GREEN August 5, 1910–July 8, 1983 BY HELMUT BEINERT, PAUL K STUMPF, AND SALIH J. WAKIL T THE TIME OF DAVID Green’s death in 1983, Frank A Huennekens, one of Green’s postdoctoral fellows, wrote in his personal recollections: David Green was a remarkable person. Endowed with a keen intellect, an insatiable curiosity about Nature, a vivid imagination and boundless en- ergy, he pursued a career devoted entirely to research. Over a period of four decades he and his colleagues published nearly 700 journal articles and reviews covering a broad spectrum of enzymology and bioenergetics. And, he was the author, co-author or editor of eight books. A legion of postdoctorals and visiting investigators received training in his laboratory. History will surely record that he was one of the giants of 20th-century biochemistry. Green’s professional career had four distinct periods, during which he explored, developed, and refined the ex- panding concepts of enzymology. They were his educational experiences at New York University and at Cambridge; his return to the United States to begin his American career for one year at Harvard; his first academic appointment at Columbia College of Physicians and Surgeons in New York City; and finally his selection as codirector of the Institute for Enzyme Research at the University of Wisconsin at Madi- son, where he remained until his untimely death in 1983.
    [Show full text]
  • Peptidyltransfer Reaction Catalyzed by the Ribosome and the Ribozyme: a Dissertation
    University of Massachusetts Medical School eScholarship@UMMS GSBS Dissertations and Theses Graduate School of Biomedical Sciences 2003-05-08 Peptidyltransfer Reaction Catalyzed by the Ribosome and the Ribozyme: a Dissertation Lele Sun University of Massachusetts Medical School Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/gsbs_diss Part of the Amino Acids, Peptides, and Proteins Commons, Cells Commons, Hormones, Hormone Substitutes, and Hormone Antagonists Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Pharmaceutical Preparations Commons, and the Therapeutics Commons Repository Citation Sun L. (2003). Peptidyltransfer Reaction Catalyzed by the Ribosome and the Ribozyme: a Dissertation. GSBS Dissertations and Theses. https://doi.org/10.13028/6ds0-4c54. Retrieved from https://escholarship.umassmed.edu/gsbs_diss/115 This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in GSBS Dissertations and Theses by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. PEPTIDYL TRANSFER REACTION CATALYZED BY THE RIBOSOME AND THE RIBOZYME A Dissertation Presented Lele Sun Submitted to the Faculty of the University of Massachusetts Graduate School of Biomedical Sciences, Worcester In partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY BIOCHEMISTRY AND MOLECULAR BIOLOGY (May 8, 2003) PEPTIDYL TRANSFER REACTION CATALYZED BY THE RIBOSOME AND THE RIBOZYME A Dissertation Presented By Lele Sun Approved as to style and content by: Dr. Tony Ip, Chair of Committee Dr. Sharon Huo, Member of Committee Dr. David Lambright, Member of Committee Dr. Craig Mello, Member of Committee Dr. Thoru Pederson, Member of Committee Dr.
    [Show full text]
  • Painful Chemistry! from Barbecue Smoke to Riot Control
    Pure Appl. Chem. 2017; 89(2): 231–248 Conference paper Christopher Green, Farrha B. Hopkins, Christopher D. Lindsay, James R. Riches and Christopher M. Timperley* Painful chemistry! From barbecue smoke to riot control DOI 10.1515/pac-2016-0911 Abstract: Pain! Most humans feel it throughout their lives. The molecular mechanisms underlying the phe- nomenon are still poorly understood. This is especially true of pain triggered in response to molecules of a certain shape and reactivity present in the environment. Such molecules can interact with the sensory nerve endings of the eyes, nose, throat and lungs to cause irritation that can range from mild to severe. The ability to alert to the presence of such potentially harmful substances has been termed the ‘common chemical sense’ and is thought to be distinct from the senses of smell or taste, which are presumed to have evolved later. Bar- becue a burger excessively and you self-experiment. Fatty acids present in the meat break off their glycerol anchor under the thermal stress. The glycerol loses two molecules of water and forms acrolein, whose assault on the eyes is partly responsible for the tears elicited by smoke. Yet the smell and taste of the burger are differ- ent experiences. It was this eye-watering character of acrolein that prompted its use as a warfare agent during World War I. It was one of several ‘lachrymators’ deployed to harass, and the forerunner of safer chemicals, such as ‘tear gas’ CS, developed for riot control. The history of development and mechanism of action of some sensory irritants is discussed here in relation to recent advice from the Scientific Advisory Board (SAB) of the Organisation for the Prohibition of Chemical Weapons (OPCW) on chemicals that conform to the definition of a riot control agent (RCA) under the Chemical Weapons Convention.
    [Show full text]
  • Frank W. Putnam 1917-2006
    FRANK W. PUTnaM 1917-2006 A Biographical Memoir by KENNETH E. NEET © 2013 National Academy of Sciences Any opinions expressed in this memoir are those of the author and do not necessarily reflect the views of the National Academy of Sciences. FRANK W. PUTnaM August 3, 1917—November 29, 2006 BY KENNETH E. NEET 1 The term “Greatest Generation” was coined by journalist Tom Brokaw to describe the cohort of people who were born before the Great Depression, took the United States through World War II, and led the country into the subsequent rebuilding/ growth years. Similar traits apply to the biomedical scientists of those times. This “Greatest Scientific Generation” was characterized by a youth spent in the Depression, an education initiated before the war, a career interrupted by (or maintained during) the war, and research accomplishments in the subsequent Cold War era largely supported by the burgeoning National Institutes of Health (NIH). Riding the subsequent wave of technology and information, this scientific FRANK W. PUTNAM FRANK W. generation led the molecular biology and molecular medicine revolutions that read like a Who’s Who of Biochemistry and Molecular Biology (Table 1). produced the complete sequencing of the human genome and is likely to culmi- Putnam remarked1 that he was fortunate to have nate in truly personalized medicine during the 21st century. participated in three intellectually stimulating collabo- rank W. Putnam was a member in good rations: the Phage Group [1947–52], the Cambridge standing of the Greatest Scientific Genera- Protein Group at the time of the double-helix discovery tion.
    [Show full text]
  • The Story of César Milstein and Monoclonal Antibodies: Introduction Page 1 of 3
    The Story of César Milstein and Monoclonal Antibodies: Introduction Page 1 of 3 A HEALTHCARE REVOLUTION IN THE MAKING The Story of César Milstein and Monoclonal Antibodies Collated and written by Dr Lara Marks Today six out of ten of the best selling drugs in the world are monoclonal antibody therapeutics. One of these, Humira®, which is a treatment for rheumatoid arthritis and other autoimmune conditions, was listed as the top selling drug across the globe in 2012 with a revenue of US$9.3 billion. Based on its current performance many predict the annual sales of the drug will surpass the peak sales of Lipitor, a treatment for lowering cholesterol, that is the best selling therapeutic of all time. Currently monoclonal antibody drugs make up a third of all new medicines introduced worldwide. 1 of 63 Celltrion, Inc., Exhibit 1024 http://www.whatisbiotechnology.org/exhibitions/milstein 9/8/2015 The Story of César Milstein and Monoclonal Antibodies: Introduction Page 2 of 3 Portrait of César Milstein. Photo credit: Godfrey Argent Studio Monoclonal antibodies are not only successful drugs, but are powerful tools for a wide range of medical applications. On the research front they are essential probes for determining the pathological pathway and cause of diseases like cancer and autoimmune and neurological disorders. They are also used for typing blood and tissue, a process that is vital to blood transfusion and organ transplants. In addition, monoclonal antibodies are critical components in diagnostics, having increased the speed and accuracy of tests. Today the antibodies are used for the detection of multiple conditions, ranging from pregnancy and heart attacks, to pandemic flu, AIDS and diseases like anthrax and smallpox released by biological weapons.
    [Show full text]
  • Clxix. Aldehyde Mutase1
    CLXIX. ALDEHYDE MUTASE1 By MALCOLM DIXON AND CECILIA LUTWAK-MANN From the Biochemical Laboratory, Cambridge (Received 28 June 1937) THE name "aldehyde mutase" is given to the enzyme which catalyses the so- called Cannizzaro reaction (reaction (1) below), a type of reaction which is probably of importance in intermediary metabolism. Batelli & Stern [1910] were the first to show that this reaction was catalysed by animal tissues, but satisfactory quantitative chemical studies were first carried out by Parnas [1910], who showed that the catalyst was a soluble enzyme, to which he gave the name of aldehyde mutase. The mutase was believed to be a separate enzyme until Wieland [1914] claimed to have shown that it was identical with the Schardinger enzyme or aldehyde oxidase, which catalyses the oxidation of aldehydes in accordance with reaction (2): (1) R-CHO + R-CHO + H20 = R-COOH + R-CH20H, (2) R-CHO + A +H20=R-COOH+AH2, where A may be 02 or some other hydrogen acceptor, such as methylene blue. Wieland suggested that the oxidase normally uses a hydrogen acceptor to produce an oxidation of the aldehyde, but when no other acceptor is present it uses a second molecule of aldehyde as acceptor, reducing it to alcohol and so producing a dismutation of aldehyde (reaction (1)). This view has been almost universally held up to the present time. The mutase has been much less thoroughly studied than the aldehyde oxidase. The main contributions to our knowledge of the enzyme are due to Euler and his co-workers [e.g. Euler & Brunius, 1928], who showed that yeast mutase requires cozymase for its activity, and to Reichel & Kohle [1935], who have recently carried out systematic studies on purified liver mutase.
    [Show full text]
  • Far Away and Long Ago
    Access provided by 181.167.139.66 on 04/23/21. For personal use only. Annu. Rev. Biochem. 1983.52:1-16. Downloaded from www.annualreviews.org .-Inn. Rev. Biochem. 1983.52: 1-15 Copyright © 1983 by Annual Reviews Inc. All rights reserved FAR AWAY AND LONG AGO Luis F. Leloir Instituto de Investigaciones Bioquimicas, "Fundacion Campomar" and Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina CONTENTS B. A. HOUSSA Y'S INSTITUTE OF PHySIOLOGy ............................ ,................. 2 INITIATION IN BIOCHEMISTRy ............. ......................... , .............. , .. , .. ,.............. 3 FATTY ACIDS ...................... ,............................... , ........... , ........ " .................... ,.......... 4 AN ADVENTURE IN HYPERTENSION , ........................ , ............ ,......................... 5 A STAY IN USA ........................ , ........ , ............ , .............................................. ,............ 7 FUNDACION CAMPOMAR .................... ....... .................... , ..... , ................... ,............ 8 DOLICHOL DERIVATIVES ......................................................................... ............. 13 WHY RESEARCH ...................... , ................... ,............................................................. 14 Biochemistry and I were born and grew at about the same time, Before the tum of the century some organic chemists and physiologists had lain the bases of Biochemistry, In 1906 two journals dealing with it appeared, the Biochemische
    [Show full text]
  • Vincent Massey 1926–2002
    Vincent Massey 1926–2002 A Biographical Memoir by David P. Ballou and Charles H. Williams, Jr. ©2013 National Academy of Sciences. Any opinions expressed in this memoir are those of the authors and do not necessarily reflect the views of the National Academy of Sciences. VINCENT MASSEY November 28, 1926–August 26, 2002 Elected to the NAS, 1995 Vincent Massey1—Vince, to all who knew him—lived life very fully. Carol Strickland, the wife of a former graduate student of Vince’s, captured his vitality when she said: “The stop-flow might have been Vince’s favorite research tool, but in life he was all flow without stop. I can still see Vince, his eyes twinkling, practically chomping the stem of his pipe in two as he gufawed at something that struck him as funny. What a bon vivant he was! Whatever he did, he did full-bore, ‘sucking all the marrow out of life,’ as Thoreau put it.” By David P. Ballou and Charles H. Williams, Jr. Vince gained international distinction in physical biochemistry. His pioneering eforts to relate favin chemistry to favin enzymology resulted in a new understanding of favin charge-transfer complexes, free radicals in favoproteins, oxygen reactivity of favins, interactions of the favin ring structure with proteins, and the classifcation of favoen- zymes. His early discovery that Straub diaphorase is in fact lipoamide dehydrogenase and that it functions as a critical component in both the pyruvate and 2-ketoglutarate dehy- drogenase complexes was a milestone in understanding metabolism. Vince’s development of totally innovative methodology for the determination of inter- mediates in enzyme catalysis through transient kinetics made favoproteins one of the best-understood enzyme families.
    [Show full text]