Purification and characterization of a lipocortin‐like 33 kDa protein from guinea pig neutrophils

FEBS Letters

Utsumi, Kozo¹  Miyahara, Masanobu¹  Sato, Eisuke F.¹ 

[1] Department of Medical Biology, Kochi Medical School, Nankoku-shi, Kochi 781-51, Japan

关键词: Amino acid composition;    Amino acid sequence;    33 kDa protein;    Lipocortin;    Phospholipase A2;   

DOI  :  10.1016/0014-5793(88)80883-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown