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Lipocortin inhibition of extracellular and intracellular phospholipases A2is substrate concentration dependent
- Source :
- FEBS Letters, 219(1), 176. Elsevier
- Publication Year :
- 1987
- Publisher :
- Wiley, 1987.
-
Abstract
- Hydrolysis of Escherichia coli membrane phospholipids by pancreatic phospholipase A2 was inhibited by lipocortin from human monocytes in a substrate dependent manner. Inhibition was completely overcome at substrate concentrations above 250 μM. Lipocortin also inhibited partially purified preparations of two intracellular phospholipases A2, isolated from rat liver mitochondria and rat platelets when these enzymes were assayed at low micromolar concentrations of phosphatidylethanolamine. Inhibition gradually decreased with increasing substrate concentrations both for pancreatic and platelet phospholipase A2 and became completely abolished above 15 and 50 μM phosphatidylethanolamine, respectively.
- Subjects :
- Blood Platelets
Diergeneeskunde
Annexins
Swine
Biophysics
Phospholipase
Biochemistry
Phospholipases A
Membrane Lipids
chemistry.chemical_compound
Phospholipase A2
Structural Biology
Escherichia coli
Genetics
Extracellular
Animals
Humans
Pancreas
Molecular Biology
Phospholipids
Glycoproteins
chemistry.chemical_classification
Phosphatidylethanolamine
Phospholipase A
biology
Hydrolysis
Phosphatidylethanolamines
Substrate (chemistry)
Cell Biology
Rats
Phospholipases A2
Enzyme
chemistry
Phospholipases
phosphatidylethanolamine
biology.protein
lipocortin
phospholipase A2
Intracellular
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 219
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....04ff406bd34dd66beedce07ae508a7ca