Proteolytic enzymes : aspartic and metallo peptidases
著者
書誌事項
Proteolytic enzymes : aspartic and metallo peptidases
(Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 248)
Academic Press, c1995
大学図書館所蔵 全92件
  青森
  岩手
  宮城
  秋田
  山形
  福島
  茨城
  栃木
  群馬
  埼玉
  千葉
  東京
  神奈川
  新潟
  富山
  石川
  福井
  山梨
  長野
  岐阜
  静岡
  愛知
  三重
  滋賀
  京都
  大阪
  兵庫
  奈良
  和歌山
  鳥取
  島根
  岡山
  広島
  山口
  徳島
  香川
  愛媛
  高知
  福岡
  佐賀
  長崎
  熊本
  大分
  宮崎
  鹿児島
  沖縄
  韓国
  中国
  タイ
  イギリス
  ドイツ
  スイス
  フランス
  ベルギー
  オランダ
  スウェーデン
  ノルウェー
  アメリカ
注記
Includes indexes
内容説明・目次
内容説明
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.
目次
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.
「Nielsen BookData」 より