Results 221 to 230 of about 296,459 (243)
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Phospholipases of marine invertebrates—I. distribution of phospholipase a

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972
Abstract 1. 1. The activities of phospholipases A, C and D were determined in the extracts of forty-six species from the main systematic groups of marine invertebrates with phosphatidyl choline, phosphatidyl ethanolamine and sphingomyelin as substrates. 2. 2. The majority of animals contained phospholipases A. 3. 3.
V E, Vaskovsky, Z S, Suppes
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Phospholipase A2—a structural review

Toxicon, 1996
Phospholipases A2 (PLA2) are widely distributed in nature and are well characterized proteins with respect to their catalytic and pharmacological activities. A wealth of structural information has recently become available both from X-ray diffraction and NMR studies, and although a detailed model of the catalytic mechanism of PLA2 has been proposed ...
Arni, R. K., Ward, R. J.
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Phospholipase C- 1: A Phospholipase and Guanine Nucleotide Exchange Factor

Molecular Interventions, 2002
Although phospholipase C-gamma (PLC-gamma) participates in cellular mitogenesis, evidence indicates that the catalytic activity of PLC-gamma (to hydrolyze certain phosphoinositides) is nonessential to the process. So how is it that PLC-gamma is necessary but its lipase activity is not?
Zhixiang, Wang, Michael F, Moran
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Group XV phospholipase A₂, a lysosomal phospholipase A₂.

Progress in lipid research, 2011
A phospholipase A₂ was identified from MDCK cell homogenates with broad specificity toward glycerophospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol. The phospholipase has the unique ability to transacylate short chain ceramides.
James A, Shayman   +4 more
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Phospholipase A2 isoforms: a perspective

Cellular Signalling, 2003
Several new PLA(2)s have been identified based on their nucleotide gene sequences. They were classified mainly into three groups: cytosolic PLA(2) (cPLA(2)), secretary PLA(2) (sPLA(2)), and intracellular PLA(2) (iPLA(2)). They differ from each other in terms of substrate specificity, Ca(2+) requirement and lipid modification.
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Assay of Phospholipase A Activity

2013
Phospholipases of the A type constitute a large family of esterases that catalyze the hydrolysis of the fatty acid ester bonds in phospholipids and thus generate lysophospholipids and fatty acids. Both products or their metabolites are important signal molecules in the cellular adaptation to stress, developmental processes and several diseases in ...
Michael, Heinze, Werner, Roos
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Phospholipase-A activity of mammalian tissues

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1965
Abstract 1. 1.The phospholipase-A (phosphatide acyl-hydrolase, EC 3.1.1.4) activity of extracts of a number of different rat tissues has been determined by estimating the decline in the concentration of lecithin together with the increase in the concentration both of fatty acids and of lysolecithin, that occurs when the extract is incubated with ...
J J, GALLAI-HATCHARD, R H, THOMPSON
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Serum phospholipase A in hematological diseases

Klinische Wochenschrift, 1989
Inflammatory cells, e.g., neutrophils, monocytes, and macrophages are presumed to be a source of circulating phospholipase A in nonpancreatic diseases. Therefore, we investigated in a preliminary study whether serum phospholipase A activity is related to leukocyte counts in 43 patients with hematological diseases.
R T, Hiefinger   +2 more
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ExoU is a potent intracellular phospholipase

Molecular Microbiology, 2004
SummaryThe combination of a large genome encoding metabolic versatility and conserved secreted virulence determinants makes Pseudomonas aeruginosa a model pathogen that can be used to study host–parasite interactions in many eukaryotic hosts. One of the virulence regulons that likely plays a role in the ability of P.
Hiromi, Sato, Dara W, Frank
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A rapid and simple phospholipase A assay

Toxicon, 1966
Abstract A simple and rapid method for the assay of phospholipase A was developed. As a substrate fresh egg yolk is used which is hydrolyzed by snake venom phospholipase A at a 10–20 × faster rate than pure lecithin. The released fatty acids, after extraction with appropriate solvents are titrated automatically.
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