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A non-secretory phospholipase A2 in the rat pancreas.

Authors: S, Durand; F, Clemente; L, Douste-Blazy;

A non-secretory phospholipase A2 in the rat pancreas.

Abstract

The rat pancreas shows a phospholipase activity in the absence of the tryptic activation of the zymogens. We verified that this activity was not due to the zymogen of the secretory phospholipase. Indeed unlike the prophospholipase, the enzyme responsible for the spontaneous phospholipase activity shows a higher catalytic rate at substrate concentrations higher than the critical micelle concentration. This enzyme has a positional specificity of the A2 type and possesses a molecular weight of about 9,500.

Keywords

Male, Phospholipases A2, Phospholipases, Phosphatidylethanolamines, Animals, Pancreas, Micelles, Phospholipases A, Rats, Substrate Specificity

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Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
7
Average
Top 10%
Top 10%
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