Proteolytic enzymes : aspartic and metallo peptidases

Bibliographic Information

Proteolytic enzymes : aspartic and metallo peptidases

edited by Alan J. Barrett

(Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 248)

Academic Press, c1995

Available at  / 92 libraries

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Includes indexes

Description and Table of Contents

Description

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.

Table of Contents

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.

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Related Books: 1-1 of 1

  • Methods in enzymology

    editors in chief, Sidney P. Colowick, Nathan O. Kaplan

    Academic Press c1955-

    v. 1 , v. 2 , v. 3 , v. 4 , v. 5 , v. 6 , v. 7 , v. 33 , v. 75 , v. 95 , v. 120 , v. 140 , v. 175 , v. 199 , v. 229 , v. 265 , v. 285 , v. 320 , v. 355

    Available at 179 libraries

Details

  • NCID
    BA25452378
  • ISBN
    • 0121821498
  • Country Code
    us
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    San Diego ; Tokyo
  • Pages/Volumes
    xxxi, 873 p.
  • Size
    24 cm
  • Classification
    • NLM : W1
  • Subject Headings
  • Parent Bibliography ID
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