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Main description:
General Description for Series:
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
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Produktbeschreibung
Main description:
General Description for Series:
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.B.M. Reid, K.F. Nolan, H.R. Linjen, and D. Collen, Introduction.

Complement Activation:
R.B. Sim, A.J. Day, B.E. Moffatt, and M. Fontaine, Complement Factor I and Cofactors in Control of Complement System Convertase Enzymes.

K.F. Nolan and K.B.M. Reid, Properdin.

A.W. Dodds, Small-Scale Preparation of Complement Components C3 and C4.

G.J. Arlaud and N.M. Thielens, Human Complement Serine Proteases Clr and Cls and Their Proenzymes.

J.E. Volanakis, S.R. Barnum, and J.M. Kilpatrick, Purification and Properties of Human Factor D.

A.E. Davis III, K.S. Aulak, K. Zahedi, J.J. Bissler, and R.A. Harrison, C1 Inhibitor.

G. Salvesen and J.J. Enghild, a-Macroglobulins: Detection and Characterization.

Fibrinolysis:
J.T. Radek, D.J. Davidson, and F.J. Castellino, Streptokinase-Plasmin(ogen) Activator Assays.

T. Trieu, D. Behnke, D. Gerlach, and J. Tang, Activation of Human Plasminogen by Recombinant Staphylokinase.

F.J. Castellino, D.J. Davidson, E. Rosen, and J. McLinden, Expression of Human Plasminogen cDNA in Lepidopteran Insect Cells and Analysis of Asparagine-Linked Glycosylation Patterns of Recombinant Plasminogens.

N. Aoki, Y. Sumi, O. Miura, and S. Hirosawa, Human a2-Plasmin Inhibitor.

H.R. Lijnen and D. Collen, Molecular Interactions between Tissue-Type Plasminogen Activator and Plasminogen.

N. Behrendt, M. Ploug, E. Ronne, G. Hoyer-Hansen, and K. Dano, Cellular Receptor for Urokinase-Type Plasminogen Activator: Protein Structure.

V. Ellis, N. Behrendt, and K. Dano, Cellular Receptor for Urokinase-Type Plasminogen Activator: Function in Cell-Surface Proteolysis.

S.J.Gardell and P.A. Friedman, Vampire Bat Salivary Plasminogen Activator.

E.L. Madison and J.F. Sambrook, Probing Structure-Function Relationships of Tissue-Type Plasminogen Activator by Oligonucleotide-Mediated Site-Specific Mutagenesis.

J.M. Edelberg, T.N. Young, and S.V. Pizzo, Lipoprotein (a): Purification and Kinetic Analysis.

Nonmammalian Blood Coagulation Factors and Inhibitors:
C.T. Dunwiddie, L. Waxman, G.P. Vlasuk, and P.A. Friedman, Purification and Characterization ofInhibitors of Blood Coagulation Factor Xa from Hematophagous Organisms.

S.R. Stone and J.M. Maraganore, Hirudin and Hirudin-Based Peptides.

T. Muta, F. Tokunaga, T. Nakamura, T. Morita, and S.D. Iwanaga, Limulus Clotting Factor C: Lipopolysaccharide-Sensitive Serine Protease Zymogen.

T. Nakamura, T. Muta, T. Oda, T. Morita, and S.D. Iwanaga, Limulus Clotting Factor B.

T. Muta, T. Nakamura, R. Hashimoto, T. Morita, and S.D. Iwanaga, Limulus Proclotting Enzyme.

S. Tanaka and S.D.Iwanaga, Limulus Test for Detecting Bacterial Endotoxins.

H. Takeya, T. Miyata, N. Nishino, T. Omori-Satoh, and S.D. Iwanaga, Snake Venom Hemorrhagic and Nonhemorrhagic Metalloendopeptidases.

F. Tokunaga and S.D. Iwanaga, Horseshoe Crab Transglutaminase.
Subject Index.
Author Index.