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Main description:
The critically acclaimed laboratory standard for more than forty years, 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. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.
Review quote:
Praise for the Volume
"This book will be a valuable addition to
…mehr

Produktbeschreibung
Main description:
The critically acclaimed laboratory standard for more than forty years, 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. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Review quote:
Praise for the Volume
"This book will be a valuable addition to any lipid library."
--Papasani V. Subbaiah, Rush Medical College of Rush University for DOODY'S PUBLISHING REVIEW
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:
Primary and Tertiary Structure:
M. Cygler and J.D. Schrag, Structure as a Basis for Understanding the Interfacial Properties of Lipases.

F. Drablos and S.B. Petersen, Identification of Conserved Residues in a Family of Esterase and Lipase Sequences.

S.B. Petersen, F. Drablos, M.T. Neves, and E.I. Petersen, Identification of Important Motifs in Protein Sequences: The Program Multim and Its Applications to Lipase Related Sequences.

J.D. Schrag and M. Cygler, Lipases and the (/( Hydrolase Fold.

C. Cambillau, Y. Bourne, M.P. Egloff, C. Martinez, and H. van Tilbeurgh, Pancreatic Lipases and Their Complexes with Colipases and Inhibitors: Crystallization and Crystal Packing.

M.R. Egmond and C.J.van Bemmel, Impact of Structural Information on Understanding Lipolytic Function.

M.T. Neves, P. Martel, E.I. Petersen, F. Drablos, and S.B. Petersen, Surface and Electrostatics of Cutinases.

Isolation, Cloning, Expression, and Engineering:
M.E. Lowe, Site-Specific Mutagenesis of Human Pancreatic Lipase.

H. Wong, R.C. Davis, J.S. Hill, D. Yang, and M. Schotz, Lipase Engineering: A Window into Structure-Function Relationships.

L. Blackberg, R.-D. Duan, and B. Sternby,Purification of Carboxyl Ester Lipase (Bile Salt-Stimulated Lipase) from Human Milk and Pancreas.

C. Schmidt-Dannert, M.L. R a, and R.D. Schmid, Two Novel Lipases from the Thermophile Bacillus thermocatenulatus: Screening, Purification, Cloning, Overexpression, and Properties.

P. Adlercreutz, T. Gitlesen, I. Ncube, and J.S. Read, Vernonia Lipase: A Plant Lipase with Strong Fatty Acid Selectivity.

J.S. Hill, R.C. Davis, D. Yang, M.C. Schotz, and H. Wong, Hepatic Lipase: High Level Expression and Subunit Structure Determination.

L. Alberghina and M. Lotti, Cloning, Sequencing, and Expression of Candida rugosa Lipases.

L. Dupuis, S. Canaan, M. Riviore, and C. Wicker-Planquart, Influence of Various Signal Peptides onSecretion of Mammalian Acidic Lipases in the Baculovirus/Insect Cell System.

C. Holm, J.A. Contreras, R. Verger, and M.C. Schotz, Large-Scale Purification and Kinetic Properties of Recombinant Hormone-Sensitive Lipase from Baculovirus/Insect Cell Systems.

M.E. Lowe, New Pancreatic Lipases: Gene Expression, Protein Secretion, and the Newborn.

M. Boston, C. Requadt, S. Danko, A. Jarnagin, E. Ashizawa, S. Wu, A.J. Poulose, and R. Bott, Structure and Function of Engineered Pseudomonas mendocina Lipase.

A. Svendsen, I.G. Clausen, S.A. Patkar, K. Borch, and M. Thellersen, Protein Engineering of Microbial Lipases with Industrial Interest.

E. Mas, M.-O. Sadoulet, A. El Battari, and D. Lombardo, Glycosylation of Bile Salt-Dependent Lipase (Cholesterol Esterase).

L. Haalck, F. Paltauf, J. Pleiss, R.D. Schmid, F. Spener, and P. Stadler, Steroselectivity of Lipase from Rhizopus oryzae toward Triacylglycerols and Analogs: Computer Aided Modeling and Experimental Validation.
Author Index.
Subject Index.