Purification and characterization of a lipocortin-like 33 kDa protein from guinea pig neutrophils.
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.
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D017302:Annexins; D006023:Glycoproteins / Q000097:blood* / Q000302:isolation & purification / Q000494:pharmacology; D006168:Guinea Pigs; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism; D009504:Neutrophils / Q000032:analysis*; D010179:Pancreas / Q000201:enzymology; D010740:Phospholipases / Q000037:antagonists & inhibitors*; D011817:Rabbits; D013552:Swine
D000199:Actins; D000596:Amino Acids; D017302:Annexins; D006023:Glycoproteins; D010740:Phospholipases