Methods: J.C. Powers and C.-M. Kam, Peptide Thioester Substrates for Serine Peptidases and Metalloendopeptidases. C.G. Knight, Fluorimetric Assays of Proteolytic Enzymes. G.M. McGeehan, D.M. Bickett, J.S. Wiseman, M. Green, and J. Berman, Defined Substrate Mixtures for Mapping of Proteinase Specificities. C.J. Handley and D.J. Buttle, Assay of Proteoglycan Degradation. J.G. Bieth, Theoretical and Practical Aspects of Proteinase Inhibition Kinetics. C.G. Knight, Active-Site Titration of Peptidases. Aspartic Peptidases: N.D. Rawlings and A.J. Barrett, Families of Aspartic Peptidases, and Those of Unknown Catalytic Mechanism. T. Kageyama, Procathepsin E and Cathepsin E. Y.P. Loh and N.X. Cawley, Processing Enzymes of Pepsin Family: Yeast Aspartic Protease 3 and Pro-opiomelanocortin Converting Enzyme. K. Takahashi, Proteinase A from Aspergillus niger. X. Lin and J. Tang, Thermopsin. K. Sankaran and H.C. Wu, Bacterial Prolipoprotein Signal Peptidase. Metallopeptidases: N.D. Rawlings and A.J. Barrett, Evolutionary Families of Metallopeptidases. D.S. Auld, Removal and Replacement of Metal Ions in Metallopeptidases. K. Morihara, Pseudolysin and Other Pathogen Endopeptidases of Thermolysin Family. C. Li and L.B. Hersh, Neprilysin: Assay Methods, Purification, and Characterization. B.P. Roques, F. Noble, P. Crine, and M.-C. Fournie-Zaluski, Inhibitors of Neprilysin: Design, Pharmacological and Clinical Applications. P. Corvol, T.A. Williams, and F. Soubrier, Peptidyl Dipeptidase A: Angiotensin I-Converting Enzyme. W. Sticker and R. Zwilling, Astacin. R.L. Wolz and J.S. Bond, Meprins A and B. J.B. Bjarnason and J.W. Fox, Snake Venom Metalloendopeptidases: Reprolysins. J.W. Fox and J.B. Bjarnason, Atrolysins: Metalloproteinases from Crotalus atrox Venom. L. Howard and P. Glynn, Membrane-Associated Metalloproteinase Recognized by Characteristic Cleavage of Myelin Basic Protein: Assay and Isolation. H. Maeda and K. Morihara, Serralysin and Related Bacterial Proteinases. M. Dioszegi, P. Cannon, and H.E. Van Wart, Vertebrate Collagenases. H. Tschesche, Human Neutrophil Collagenase. H. Nagase, Human Stromelysins 1 and 2. G. Murphy and T. Crabbe, Gelatinases A and B. J.F. Woessner, Jr., Matrilysin. G. Murphy and F. Willenbrock, Tissue Inhibitors of Matrix Metalloendopeptidases. J.F. Woessner, Jr., Quantification of Matrix Metalloproteinases in Tissue Samples. A.J. Barrett, M.A. Brown, P.M. Dando, C.G. Knight, N. McKie, N.D. Rawlings, and A. Serizawa, Thimet Oligopeptidase and Oligopeptidase M. G. Isaya and F. Kalousek, Mitochondrial Intermediate Peptidase. C.A. Conlin and C.G. Miller, Dipeptidyl Carboxypeptidase and Oligopeptidase A from Escherichia coli and Salmonella typhimurium. V. Monnet, Oligoendopeptidases from Lactococcus lactis. F. Checler, H. Barelli, P. Dauch, V. Dive, B. Vincent, and J.P. Vincent, Neurolysin: Purification and Assays. J. Bouvier, P. Schneider, and R. Etges, Leishmanolysin: Surface Metalloproteinase of Leishmania. A.G. Plaut and A. Wright, Immunoglobulin A-Metallo-Type Specific Prolyl Endopeptidases. G. Schiavo and C. Montecucco, Tetanus and Botulism Neurotoxins: Isolation and Assay. R.A. Skidgel, Human Carboxypeptidase N: Lysine Carboxypeptidase. F. Tan, P.A. Deddish, and R.A. Skidgel, Human Carboxypeptidase M. V.M. Stepanov, Carboxypeptidase T. A. Anastasi and A.J. Barrett, Pitrilysin. A.B. Becker and R.A. Roth, Insulysin and Pitrilysin: Insulin-Degrading Enzymes of Mammals and Bacteria. P. Cohen, A.R. Pierotti, V. Chesneau,T. Foulon, and A. Prat, N-Arginine Dibasic Convertase. M. Brunner and W. Neupert, Purification and Characterization of Mitochondrial Processing Peptidase of Neurospora crassa. A. Mellors and R.Y.C. Lo, O-Sialoglycoprotease from Pasteurella haemolytica. E. Kessler, Beta-Lytic Endopeptidases. K.E. Kadler, S.J. Lightfoot, and R.B. Watson, Procollagen N-Peptidases: Procollagen N-Proteinases. K.E. Kadler and R.B. Watson, Procollagen C-Peptidase: Procollagen C-Proteinase. M.-L. Hagmann, U. Geuss, S. Fischer, and G.-B. Kresse, Peptidyl-Asp Metalloendopeptidase. Author Index. Subject Index.
In this volume of Methods in Enzymology and its companion Volume 244, the chapters on specific methods, enzymes, and inhibitors are organized within the rational framework of the new systems for classificationand nomenclature. A wide variety of specificities of peptide bond hydrolysis are represented in each set of peptidases, together with an equally wide range of biological functions.
@introbul:Key Features @bul:* Aspartic peptidases
- New information on classification of proteolytic enzymes
- Medical implications of research in this area
- Biotechnological uses of these enzymes
Biochemists, molecular biologists, cell biologists, microbiologists, physiologists, neuroscientists, and immunologists.
- No. of pages:
- © Academic Press 1995
- 22nd June 1995
- Academic Press
- eBook ISBN:
@from:Praise for the Volume @qu:"Because this is a very significant and timely review, this book is a worthy contribution to any chemical, biological, or medical library for those interested not only in proteases but also their physiologic roles in matrix degradation and post-translational processing." @source:--DOODY'S JOURNAL @from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Wellcome Trust Sanger Institute, Cambridge, U.K.
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