The solubilization of platelet membrane-bound acetylcholinesterase and aryl acylamidase by exogenous or endogenous phosphatidylinositol specific phospholipase C.

Abstract:

:Phosphatidylinositol specific phospholipase C from Staphylococcus aureus could solubilize acetylcholinesterase up to 55% from sheep platelets in the presence of ethylenediaminetetra acetic acid (EDTA). The endogenous phosphatidylinositol specific phospholipase C of platelets activated by deoxycholate (at 3-5 mM) could also solubilize the enzyme to a similar extent. The solubilized enzyme could be further purified to apparent homogeneity by affinity chromatography without the use of any detergents. It is suggested that phosphatidylinositol specific phospholipase C will be a useful tool in the solubilization of acetylcholinesterase from mammalian sources and its purification free of detergents. The present study also demonstrates the parallel behaviour of acetylcholinesterase and aryl acylamidase in platelets confirming their identity.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Majumdar R,Balasubramanian AS

doi

10.1016/0006-2952(85)90202-3

subject

Has Abstract

pub_date

1985-12-01 00:00:00

pages

4109-15

issue

23

eissn

0006-2952

issn

1873-2968

pii

0006-2952(85)90202-3

journal_volume

34

pub_type

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