{"title":"人多形核白细胞钙依赖性蛋白水解活性的鉴定。","authors":"J L Legendre, H P Jones","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Calcium-dependent proteolytic activity has been identified in extracts of human polymorphonuclear leukocytes. The activity is most pronounced in the neutral pH range with a pH optimum of 7.3. Maximal activation of the protease occurs at a free calcium concentration of 190 microM; it is half maximal at 91 microM. This protease activity is strongly inhibited by aprotinin and phenylmethylsulfonyl fluoride (PMSF) and more weakly inhibited by antipain, leupeptin, and o-phenanthroline. The protease is not activated by calmodulin nor is it inhibited by the calmodulin antagonist trifluoperazine. Gel filtration suggests a molecular weight of 74,100 daltons.</p>","PeriodicalId":17481,"journal":{"name":"Journal of the Reticuloendothelial Society","volume":"34 2","pages":"89-97"},"PeriodicalIF":0.0000,"publicationDate":"1983-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification of calcium-dependent proteolytic activity in human polymorphonuclear leukocytes.\",\"authors\":\"J L Legendre, H P Jones\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Calcium-dependent proteolytic activity has been identified in extracts of human polymorphonuclear leukocytes. The activity is most pronounced in the neutral pH range with a pH optimum of 7.3. Maximal activation of the protease occurs at a free calcium concentration of 190 microM; it is half maximal at 91 microM. This protease activity is strongly inhibited by aprotinin and phenylmethylsulfonyl fluoride (PMSF) and more weakly inhibited by antipain, leupeptin, and o-phenanthroline. The protease is not activated by calmodulin nor is it inhibited by the calmodulin antagonist trifluoperazine. Gel filtration suggests a molecular weight of 74,100 daltons.</p>\",\"PeriodicalId\":17481,\"journal\":{\"name\":\"Journal of the Reticuloendothelial Society\",\"volume\":\"34 2\",\"pages\":\"89-97\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1983-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Reticuloendothelial Society\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Reticuloendothelial Society","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Identification of calcium-dependent proteolytic activity in human polymorphonuclear leukocytes.
Calcium-dependent proteolytic activity has been identified in extracts of human polymorphonuclear leukocytes. The activity is most pronounced in the neutral pH range with a pH optimum of 7.3. Maximal activation of the protease occurs at a free calcium concentration of 190 microM; it is half maximal at 91 microM. This protease activity is strongly inhibited by aprotinin and phenylmethylsulfonyl fluoride (PMSF) and more weakly inhibited by antipain, leupeptin, and o-phenanthroline. The protease is not activated by calmodulin nor is it inhibited by the calmodulin antagonist trifluoperazine. Gel filtration suggests a molecular weight of 74,100 daltons.
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