Purification and characterization of membrane-bound phospholipase A2 from rat platelets.

Abstract:

:Phospholipase A2 was solubilized from rat platelet membrane by 1 M KCl and purified to near homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and HPLC. The characteristics of the purified membrane-bound enzyme were compared with those of phospholipase A2 released from thrombin-stimulated rat platelets (Horigome, K., Hayakawa, M., Inoue, K., & Nojima, S. (1987) J. Biochem. 101, 625-631). The molecular weights, elution profiles on reversed-phase HPLC, and NH2-terminal sequences were identical for the two enzymes. Other characteristics of the two enzymes, such as specific activity, substrate specificity, pH optimum, Ca2+ requirement, heat lability, and sensitivity to p-bromophenacyl bromide were also indistinguishable. These findings suggest that both enzymes share a common structure.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hayakawa M,Kudo I,Tomita M,Inoue K

doi

10.1093/oxfordjournals.jbchem.a122258

subject

Has Abstract

pub_date

1988-02-01 00:00:00

pages

263-6

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

103

pub_type

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