Enzymology at the Membrane Interface: Interfacial Enzymology and Protein-Membrane Binding: Volume 583

Enzymology at the Membrane Interface: Interfacial Enzymology and Protein-Membrane Binding: Volume 583

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Description

Enzymology at the Membrane Interface, the latest volume in the Methods in Enzymology series, covers a subset of enzymes that work in the environment of the biological cell membrane. This field, called interfacial enzymology, involves a special series of experimental approaches for the isolation and study of these enzymes.
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Product details

  • Hardback | 430 pages
  • 152 x 229 x 23.88mm | 840g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 0128094192
  • 9780128094198

Table of contents

A High-Throughput Flurometric Assay for Lipid-Protein Binding
Wonhwa Cho
Fluorescence-based in situ quantitative imaging for cellular lipids
Wonhwa Cho
Recombinant Expression of human and mouse groups I, II, III, V, V and XII Secreted Phospholipases A2
Michael H. Gelb and Gerard Lambeau
Vesicle-based assay of secreted phospholipase A2 enzymatic activity for high throughput screening of compound libraries
Michael H. Gelb
Cellular Assays for Evaluating Calcium-Dependent Translocation of cPLA2a to Membrane
Christina C. Leslie
Secreted Phospholipase A2 Specificity on Natural Membrane Phospholipids
Makoto Murakami
Analyses of Calcium-Independent Phospholipase A2beta (iPLA2ss) in Biological Systems
Sasanka Ramanadham
Using hydrogen deuterium exchange mass spectrometry to examine protein membrane interactions
John E. Burke
Lipid-binding C2 domains mediate a diverse class of enzymatic functions"
Robert V. Stahelin
Interfacial Enzymes: Membrane Binding, Orientation, Membrane Insertion, and Activity
Suren Tatulian
Enzymology at the Membrane Interface
Dan M. Raben
Studying gastric lipase adsorption onto phospholipid monolayers by surface tensiometry, ellipsometry and atomic force microscopy
Frederic Carriere
Probing conformational changes and interfacial recognition site of lipases with surfactants and inhibitors
Frederic Carriere
Measuring Phospholipase D enzymatic activity through biochemical and imaging methods
Michael A. Frohman
Pld Rotein-Protein Interaction with Intracellular Signaling Molecules, Modulation by Mitogen Pa and Pld's Gef Activity
Julian G. Cambronero
Phosphatidic Acid Regulation of PIPKI
Guangwei Du
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About Michael H Gelb

Michael H. Gelb studied chemistry and biochemistry as an undergraduate at the University of California at Davis. His Ph.D. studies with Stephen G. Sligar at Yale University led to a better understanding of the catalytic mechanism of cytochrome P450. As an American Cancer Society Postdoctoral Fellow in the laboratory of the late Robert H. Abeles at Brandeis University, Gelb studied a variety of mechanism-based inactivators of serine proteases and developed fluorinated ketones as tight-binding inhibitors of several classes of proteases. In 1985 Gelb became a faculty member in the Departments of Chemistry and Biochemistry at the University of Washington. Major breakthroughs in the group include the development of methods to properly analyze the action of enzymes on membrane surfaces, the discovery of protein prenylation (farnesylation and geranylgeranylation) in mammalian cells (together with John A. Glomset), the development of Isotope-Coded Affinity Tags (ICAT reagents) for proteomic applications (together with Ruedi Aebersold), and the development of newborn screening for lysosomal storage diseases by mass spectrometry.
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