Main description:
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.
Review quote:
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"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."
--BIO/TECHNOLOGY
"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."
--CHEMISTRY IN INDUSTRY
"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."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"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."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
K.G. Mann and L. Lorand, Introduction: Blood Coagulation.
L. Patthy, Modular Design of Proteases of Coagulation, Fibrinolysis, and Complement Activation: Implications for Protein Engineering and Structure-Function Studies.
L. Lorand, J.-M. Jeong, J.T. Radek, and J. Wilson, Human Plasma Factor XIII: Subunit Interactions and Activation of Zymogen.
A. Ichinose and H. Kaetsu, Molecular Approach to Structure-Function Relationships of Human Coagulation FactorXIII.
R.A. Pixley and R.W. Colman, Factor XII: Hageman Factor.
P.N. Walsh, F.A. Baglia, and B.A. Jameson, Factor XI: Structure-Function Relationship Utilizing Monoclonal Antibodies, Protein Modification, Computational Chemistry, and Rational Synthetic Peptide Design.
S.P. Bajaj and J.J. Birktoft, Human Factor IX and Factor IXa.
P. Lollar, P.J. Fay, and D.N. Fass, Factor VIII and Factor VIIIa.
A.R. Thompson and S.-H. Chen, Characterization of Factor IX Defects in Hemophilia BPatients.
L.W. Hoyer, Characterization of Dysfunctional Factor VIII Molecules.
J.H. Lawson, S. Krishnaswamy, S. Butenas, and K.G. Mann, Proteolytic Activity of Extrinsic Pathway.
T.J. Girard and G.J. Broze, Jr., Tissue Factor Pathway Inhibitor.
W. Ruf, D.J. Miles, A. Rehemtulla, and T.S. Edgington, Mutational Analysis of Receptor and Cofactor Function of Tissue Factor.
M. Kalafatis, S. Krishnaswamy, M.D. Rand, and K.G. Mann, Factor V.
D.D. Pittman and R.J. Kaufman, Site-Directed Mutagenesis and Expression of Coagulation Factors VIII and V in Mammalian Cells.
S. Krishnaswamy, M.E. Nesheim, E.L.G. Pryzdial, and K.G. Mann, Assembly of Prothrombinase Complex.
P.B. Tracy, R.A. Robinson, L.A. Worfolf, and D.H. Allen, Procoagulant Activities Expressed by Peripheral Blood Mononuclear Cells.
M.F. Doyle and P.E. Haley, Meizothrombin: Active Intermediate Formed during Prothrombinase-Catalyzed Activation of Prothrombin.
R.A. Henriksen, Identification and Characterization of Mutant Thrombins: Structure-Function Relationships.
S. Okamoto and A. Hijikata-Okunomiya, Synthetic Selective Inhibitors of Thrombin.
A.S. Ng, S.D. Lewis, and J.A. Shafer, Quantifying Thrombin-Catalyzed Release of Fibrinopeptide from Fibrinogen Using High-Performance Liquid Chromatography.
C.T. Esmon, N.L. Esmon, B.F. Le Bonniec, and A.E. Johnson, Protein C Activation.
K. Suzuki, Protein C Inhibitor.
R.J. Jenny, T.L. Messier, L.A. Ouellette, and W.R. Church, Immunochemical Techniques for Studying Coagulation Proteins.
C. Valcarce, E. Persson, J. Astermark, A.-K. Khlin, and J. Stenflo, Isolation of Intact Modules from Noncatalytic Parts of Vitamin K-Dependent Coagulation Factors IX and X and Protein C.
K.J. Kotkow, D.A. Roth, T.J. Porter, B.C. Furie, and B. Furie, Role of Propeptide in Vitamin K-Dependent g-Carboxylation.
K.L. Berkner, Expression of Recombinant Vitamin K-Dependent Proteins in Mammalian Cells: Factors IX and VII.
P.E. Bock, Thioester Peptide Chloromethyl Ketones: Reagents for Active Site-Selective Labeling of Serine Proteinases.
E.B. Williams and K.G. Mann, Peptide Chloromethyl Ketones as Labeling Reagents.
R.P. Tracy, R. Jenny, E.B. Williams, and K.G. Mann, Active Site-Specific Assays for Enzymes of Coagulation and Fibrinolytic Pathways.
S.T. Olson, I. Bjirk, and J.D. Shore, Kinetic Characterization of Heparin-Catalyzed and Uncatalyzed Inhibition of Blood Coagulation Proteinases by Antithrombin.
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.
Review quote:
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"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."
--BIO/TECHNOLOGY
"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."
--CHEMISTRY IN INDUSTRY
"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."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"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."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
K.G. Mann and L. Lorand, Introduction: Blood Coagulation.
L. Patthy, Modular Design of Proteases of Coagulation, Fibrinolysis, and Complement Activation: Implications for Protein Engineering and Structure-Function Studies.
L. Lorand, J.-M. Jeong, J.T. Radek, and J. Wilson, Human Plasma Factor XIII: Subunit Interactions and Activation of Zymogen.
A. Ichinose and H. Kaetsu, Molecular Approach to Structure-Function Relationships of Human Coagulation FactorXIII.
R.A. Pixley and R.W. Colman, Factor XII: Hageman Factor.
P.N. Walsh, F.A. Baglia, and B.A. Jameson, Factor XI: Structure-Function Relationship Utilizing Monoclonal Antibodies, Protein Modification, Computational Chemistry, and Rational Synthetic Peptide Design.
S.P. Bajaj and J.J. Birktoft, Human Factor IX and Factor IXa.
P. Lollar, P.J. Fay, and D.N. Fass, Factor VIII and Factor VIIIa.
A.R. Thompson and S.-H. Chen, Characterization of Factor IX Defects in Hemophilia BPatients.
L.W. Hoyer, Characterization of Dysfunctional Factor VIII Molecules.
J.H. Lawson, S. Krishnaswamy, S. Butenas, and K.G. Mann, Proteolytic Activity of Extrinsic Pathway.
T.J. Girard and G.J. Broze, Jr., Tissue Factor Pathway Inhibitor.
W. Ruf, D.J. Miles, A. Rehemtulla, and T.S. Edgington, Mutational Analysis of Receptor and Cofactor Function of Tissue Factor.
M. Kalafatis, S. Krishnaswamy, M.D. Rand, and K.G. Mann, Factor V.
D.D. Pittman and R.J. Kaufman, Site-Directed Mutagenesis and Expression of Coagulation Factors VIII and V in Mammalian Cells.
S. Krishnaswamy, M.E. Nesheim, E.L.G. Pryzdial, and K.G. Mann, Assembly of Prothrombinase Complex.
P.B. Tracy, R.A. Robinson, L.A. Worfolf, and D.H. Allen, Procoagulant Activities Expressed by Peripheral Blood Mononuclear Cells.
M.F. Doyle and P.E. Haley, Meizothrombin: Active Intermediate Formed during Prothrombinase-Catalyzed Activation of Prothrombin.
R.A. Henriksen, Identification and Characterization of Mutant Thrombins: Structure-Function Relationships.
S. Okamoto and A. Hijikata-Okunomiya, Synthetic Selective Inhibitors of Thrombin.
A.S. Ng, S.D. Lewis, and J.A. Shafer, Quantifying Thrombin-Catalyzed Release of Fibrinopeptide from Fibrinogen Using High-Performance Liquid Chromatography.
C.T. Esmon, N.L. Esmon, B.F. Le Bonniec, and A.E. Johnson, Protein C Activation.
K. Suzuki, Protein C Inhibitor.
R.J. Jenny, T.L. Messier, L.A. Ouellette, and W.R. Church, Immunochemical Techniques for Studying Coagulation Proteins.
C. Valcarce, E. Persson, J. Astermark, A.-K. Khlin, and J. Stenflo, Isolation of Intact Modules from Noncatalytic Parts of Vitamin K-Dependent Coagulation Factors IX and X and Protein C.
K.J. Kotkow, D.A. Roth, T.J. Porter, B.C. Furie, and B. Furie, Role of Propeptide in Vitamin K-Dependent g-Carboxylation.
K.L. Berkner, Expression of Recombinant Vitamin K-Dependent Proteins in Mammalian Cells: Factors IX and VII.
P.E. Bock, Thioester Peptide Chloromethyl Ketones: Reagents for Active Site-Selective Labeling of Serine Proteinases.
E.B. Williams and K.G. Mann, Peptide Chloromethyl Ketones as Labeling Reagents.
R.P. Tracy, R. Jenny, E.B. Williams, and K.G. Mann, Active Site-Specific Assays for Enzymes of Coagulation and Fibrinolytic Pathways.
S.T. Olson, I. Bjirk, and J.D. Shore, Kinetic Characterization of Heparin-Catalyzed and Uncatalyzed Inhibition of Blood Coagulation Proteinases by Antithrombin.
Author Index.
Subject Index.