Purification and Some Properties of Membrane-Associated Phospholipase A(2) of Human Spleen
- 1 July 1986
- journal article
- research article
- Published by S. Karger AG in Enzyme
- Vol. 35 (1) , 2-12
- https://doi.org/10.1159/000469312
Abstract
Membrane-associated phospholipase A(2) was purified to homogeneity from human spleen. The enzyme was solubilized from the particulate fraction by the addition of KBr, and purified by reverse-phase high-performance liquid chromatography. The estimated molecular weight of the enzyme was 14,000. The enzyme had a pH optimum around 9.5, required the presence of Ca^2+ for its activity, and hydrolyzed phosphatidylethanolamine more efficiently than phosphatidylcholine.Keywords
This publication has 0 references indexed in Scilit: