The chymotrypsin inhibitor carbobenzyloxy-leucine-tyrosine-chloromethylketone interferes with phospholipase D activation induced by formyl-methionyl-leucyl-phenylalanine in human neutrophils-Reference-Cited by-同舟云学术

The chymotrypsin inhibitor carbobenzyloxy-leucine-tyrosine-chloromethylketone interferes with phospholipase D activation induced by formyl-methionyl-leucyl-phenylalanine in human neutrophils

Published:1991-08 Issue:24 Volume:266 Page:15870-15875
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kessels G.C.,Gervaix A.,Lew P.D.,Verhoeven A.J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Structural and catalytic properties of the solubilized superoxide-generating activity of human polymorphonuclear leukocytes. Solubilization, stabilization in solution, and partial characterization

2. The O2(-) -forming oxidase responsible for the respiratory burst in human neutrophils. Properties of the solubilized enzyme.

3. Activation of a NADPH Oxidase From Horse Polymorphonuclear Leukocytes in a Cell- Free System

4. Activation of NADPH-dependent superoxide production in a cell-free system by sodium dodecyl sulfate.

5. Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system.

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