{"title":"马血液白细胞中弹性酶样蛋白酶的分离及性质研究。","authors":"J Potempa","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The rapid, two steps method of purification of an elastase-like proteinase from cytoplasmic granules of horse leucocytes is described. This enzyme called the proteinase 1 is released easily from isolated granules in the low ionic strength solutions in opposite to the other two molecular forms of which one differs slightly in isoelectric point from the other. The enzyme is a typical neutral proteinase of a broad substrate specificity and wide pH optimum. In a physiological conditions the enzyme is built of two polypeptide chains of molecular weight about 30000 and 20000, respectively.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 1-2","pages":"41-52"},"PeriodicalIF":0.0000,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Isolation and properties of an elastase-like proteinase from horse blood leucocytes.\",\"authors\":\"J Potempa\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The rapid, two steps method of purification of an elastase-like proteinase from cytoplasmic granules of horse leucocytes is described. This enzyme called the proteinase 1 is released easily from isolated granules in the low ionic strength solutions in opposite to the other two molecular forms of which one differs slightly in isoelectric point from the other. The enzyme is a typical neutral proteinase of a broad substrate specificity and wide pH optimum. In a physiological conditions the enzyme is built of two polypeptide chains of molecular weight about 30000 and 20000, respectively.</p>\",\"PeriodicalId\":75854,\"journal\":{\"name\":\"Folia histochemica et cytochemica\",\"volume\":\"20 1-2\",\"pages\":\"41-52\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Folia histochemica et cytochemica\",\"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":"Folia histochemica et cytochemica","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Isolation and properties of an elastase-like proteinase from horse blood leucocytes.
The rapid, two steps method of purification of an elastase-like proteinase from cytoplasmic granules of horse leucocytes is described. This enzyme called the proteinase 1 is released easily from isolated granules in the low ionic strength solutions in opposite to the other two molecular forms of which one differs slightly in isoelectric point from the other. The enzyme is a typical neutral proteinase of a broad substrate specificity and wide pH optimum. In a physiological conditions the enzyme is built of two polypeptide chains of molecular weight about 30000 and 20000, respectively.
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