Abstract:
:We can detect phospholipase A activity in non-hemolyzed sheep erythrocytes, using dilauroylglycerophosphocholine as an exogenous substrate. Only substrates such as dilauroylglycerophosphocholine, which can be incorporated into membranes, could be hydrolyzed by the enzyme, egg phosphatidylcholine being only slightly sensitive to the enzyme in the absence of detergent. Egg phosphatidylcholine is not hydrolyzed even in the presence of dilauroylglycerophosphocholine at the concentration used routinely in the present experiment, indicating that dilauroylglycerophosphocholine itself does not behave as a detergent under the present experimental conditions. Exogenous calcium ions are necessary for the activity, but it was abolished by EDTA. This finding suggests that the Ca2+ binding site of the enzyme may be exposed on the outer surface of the erythrocyte membrane.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Tanaka Y,Eriomin VA,Kawamura Y,Inoue K,Nojima Sdoi
10.1093/oxfordjournals.jbchem.a134426subject
Has Abstractpub_date
1983-09-01 00:00:00pages
841-7issue
3eissn
0021-924Xissn
1756-2651journal_volume
94pub_type
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