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Purification and characterization of a lipocortin-like 33 kDa protein from guinea pig neutrophils
E F Sato1, M Miyahara, K Utsumi
1Department of Medical Biology, Kochi Medical School, Japan.
FEBS Letters
|January 25, 1988
Abstract:
A lipocortin-like, phospholipase A2 inhibitory 33 kDa protein was purified from guinea pig neutrophils. From amino acid composition and sequence data, this protein was found to have a high degree of homology to human lipocortin I. This protein inhibited porcine pancreatic phospholipase A2 activity in the presence of [3H]oleic acid-labeled Escherichia coli membranes as substrate. Maximal inhibition amounted to 65% whereas 50% inhibition occurred at 83.5 nM. This protein showed F-actin-binding ability in a Ca2+-dependent manner.