A.J. Barrett, Classification of Peptidases.
N.D. Rawlings and A.J. Barrett, Families of Serine Peptidases.
J.R. Hoidal, N.V. Rao, and B. Gray, Myeloblastin: Leukocyte Proteinase 3.
M.M. Simon and M.D. Kramer, Granzyme A.
M.C. Peitsch and J. Tschopp, Granzyme B.
L.B. Schwartz, Tryptase: A Mast Cell Serine Protease.
K. Kurachi, A. Torres-Rosado, and A. Tsuji, Hepsin.
J.J. Birktoft and K. Breddam, Glutamyl Endopeptidases.
F. Sakiyama and T. Masaki, Lysyl Endopeptidase of Achromobacter lyticus.
A.G. Plaut and W.W. Bachovchin, IgA-Specific Prolyl Endopeptidases: Serine Type.
C. Brenner, A. Bevan, and R.S. Fuller, Biochemical and Genetic Methods for Analyzing Specificity and Activity of Precursor-Processing Enzyme: Yeast Kex2 Protease, Kexin.
K. Nakayama, Purification of Recombinant Soluble Forms of Furin Produced in Chinese Hamster Ovary Cells.
N.G. Seidah and M. Chretien, Pro-Protein Convertases of Subtilisin/Kexin Family.
L. Polgar, Prolyl Oligopeptidases.
D. Tsuru and T. Yoshimoto, Oligopeptidase B: Protease II from Escherichia coli.
Y. Ikehara, S. Ogata, and Y. Misumi, Dipeptidyl-peptidase IV from Rat Liver.
W.M. Jones, A. Scaloni, and J.M. Manning, Acylaminoacyl-peptidase.
S.J. Remington and K. Breddam, Carboxypeptidases C and D.
B. Granier, M. Jamin, M. Adam, M. Galleni, B. Lakaye, W. Zorzi, J. Grandchamps, J.-M. Wilkin, C. Fraipont, B. Joris, C. Duez, M. Nguyen-Distoche, J. Coyette, M. Leyh-Bouille, J. Dusart, L. Christiaens, J.-M. Frore, and J.-M. Ghuysen, Serine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins.
J.W. Little, B. Kim, K.L. Roland, M.H. Smith, L.-L. Lin, and S.N. Slilaty, Cleavage of LexA Repressor.
W.R. Tschantz and R.E. Dalbey, Bacterial Leader Peptidase 1.
M.O. Lively, A.L. Newsome, and M. Nusier, Eukaryote Microsomal Signal Peptidases.
M.R. Maurizi, M.W. Thompson, S.K. Singh, and S.-H. Kim, Endopeptidase Clp: ATP-Dependent Clp Protease from Escherichia coli.
A.J. Rivett, P.J. Savory, and H. Djaballah, Multicatalytic Endopeptidase Complex: Proteasome.
A.L. Goldberg, R.P. Moerschell, C.H. Chung, and M.R. Maurizi, ATP-Dependent Protease La (Lon) from Escherichia coli.
S. Kuzela and A.L. Goldberg, Mitochondrial ATP-Dependent Protease from Rat Liver and Yeast.
W.F. Mangel, D.L. Toledo, M.T. Brown, K. Worzalla, M. Lee, and J.J. Dunn, Omptin: An Escherichia coli Outer Membrane Proteinase That Activates Plasminogen.
W. Gibson, A.R. Welch, and J. Ludford, Transient Transfection Assay of the Herpesvirus Maturational Proteinase, Assemblin.
M.C. Smith, J. Giordano, J.A. Cook, M. Wakulchik, E.C. Villarreal, G.W. Becker, K. Bemis, J. Labus, and J.S. Manetta, Purification and Kinetic Characterization of Human Cytomegalovirus Assemblin.
J. Oleksyszyn and J.C. Powers, Amino Acid and Peptide Phosphonate Derivatives as Specific Inhibitors of Serine Peptidases.
J.C. Powers and C.-M. Kam, Isocoumarin Inhibitors of Serine Peptidases.
N.D. Rawlings and A.J. Barrett, Families of Cysteine Peptidases.
A.C. Storer and R. Menard, Catalytic Mechanism in Papain Family of Cysteine Peptidases.
H. Kirschke and B. Wiederanders, Cathepsin S and Related Lysosomal Endopeptidases.
H. Scholze and E. Tannich, Cysteine Endopeptidases of Entamoeba histolytica.
M.J. North, Cysteine Endopeptidases of Parasitic Protozoa.
D.J. Buttle, Glycyl Endopeptidase.
A.D. Rowan and D.J. Buttle, Pineapple Cysteine Endopeptidases.
S.G. Gordon, Cancer Procoagulant.
T. Skern and H.-D. Liebig, Picornains 2A and 3C.
J.M. Weber and K. Tihanyi, Adenovirus Endopeptidases.
S-I. Ishii, Legumain: Asparaginyl Endopeptidase.
N.A. Thornberry, Interleukin-1( Converting Enzyme.
R.R. Rando and Y.-T. Ma, Isoprenylated Protein Endopeptidase.
D.J. Buttle, Affinity Chromatography of Cysteine Peptidases.
E. Shaw, Peptidyl Diazomethanes as Inhibitors of Cysteine and Serine Proteinases.
A. Krantz, Peptidyl (Acyloxy)methanes as Quiescent Affinity Labels for Cysteine Proteinases.
D. Brimme and H.-U. Demuth, N,O-Diacyl Hydroxamates as Selective and Irreversible Inhibitors of Cysteine Proteinases.
M. Abrahamson, Cystatins. Author Index. Subject Index.
The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
@introbul:Key Features @bul:* Presents new ideas on classification of proteolytic enzymes
- Covers 100 individual proteolytic enzymes
- Offers numerous medical implications of work in this area
- Provides uses of these enzymes in biotechnology
Biochemists, molecular biologists, cell biologists, microbiologists, physiologists, neuroscientists, and immunologists.
- No. of pages:
- © Academic Press 1994
- 8th November 1994
- Academic Press
- eBook ISBN:
- Hardcover ISBN:
@from:Praise for the Volume @qu:"Indeed, the volume encompasses not only preparation, assay, and function, but also a remarkably rich lode of information on the underlying biology of the tissues, microorganisms, and viruses that are the sources of the peptidasesunder discussion... This volume is a welcome and valuable addition to the biochemist's library." @source:--ANALYTICAL BIOCHEMISTRY @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
Wellcome Trust Sanger Institute, Cambridge, U.K.
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA