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Proteinaceous inhibitors of phospholipase A₂ purified from inflammatory sites in rats
SUWA, YORIMAS,KUDO, ICHIRO,IMAIZUMI, ATSUSHI,OKADA, MASAHIRO,KAMIMURA, TAKASHI,SUZUKI, YOJI,CHANG, HYEUN WOOK,HARA, SHUNTARO,INOUE, KEIZO 영남대학교 약품개발연구소 1991 영남대학교 약품개발연구소 연구업적집 Vol.1 No.-
We have purified two phospholipase A₂ inhibitory proteins (37 and 33 kDa) from peritoneal fluid of dexamethasone-treated rats. The extracellular phospholipase A₂ round in inflammatory sites differed from the exocrine phospholipase A₂ in susceptibility to these endogenous inhibitors; both proteins inhibited the activity of the extracellular phospholipase A₂ purified from sites of inflammation but did not affect appreciably the activity of either porcine pancreatic or Naja naja venom phospholipase A₂. The amino acid sequence of the NH₂-terminal portion of the purified proteins did not resemble that of lipocortins so far reported, but it was almost identical to that of parts of human or mouse complement component C3. These findings may indicate that degraded products of C3 are involved in the regulation of activity of a class of mammalian phospholipase A₂.
백석환,다까야마기요시,구도이찌로,이노우에게이조,이현우,도준영,장현욱 영남대학교 약품개발연구소 1992 영남대학교 약품개발연구소 연구업적집 Vol.2 No.-
Extracellular phospholipase A₂ activity has been identified in pleural fluid of patients with tuberculosis. This enzyme is a calcium requiring protein and has a pH optimum of 10.0. The enzyme was inhibited by the active site-directed histidine reagent, p-bromophenacyl bromide, lonic and non-ionic detergents, or the sulfhydryl reagent dithiothreitol, caused loss of enzyme activity. When substrate specificity was tested using 2-[1-^(l4)C]linoleoyl phospholipids as substrates, phosphatidyl-ethanolamine was the best substrate, followed by phosphatidylserine and phosphatidylcholine. This phospholipase A₂ showed high affinity for heparin, and was recognized by a monoclonal antibody raised against phospholipase A₂ from human synovial fluid. These findings suggest that an extracellular phospholipase A₂, which may belong to the 14K group Ⅱ phospholipase A₂ family, exists in the pleural fluid of patients with tuberculosis.