{"title":"海洋源性低温蛋白酶的分离纯化及初步鉴定。","authors":"M H Salamanca, C Barría, J A Asenjo, B A Andrews","doi":"10.1023/a:1016383212244","DOIUrl":null,"url":null,"abstract":"<p><p>The isolation and preliminary characterization of a trypsin-like protease with high activity at 20 degrees C is described. This protease was isolated from Antarctic krill (Euphasia superba) by a two-step chromatography process and the use of zymogram analyses. The protease has a molecular weight of 30 kDa and a pI of 4.1. Its specific activity at 20 degrees C on BAPNA is 0.5 U/mg.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"10 4-5","pages":"237-41"},"PeriodicalIF":0.0000,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1016383212244","citationCount":"13","resultStr":"{\"title\":\"Isolation, purification and preliminary characterization of cryophilic proteases of marine origin.\",\"authors\":\"M H Salamanca, C Barría, J A Asenjo, B A Andrews\",\"doi\":\"10.1023/a:1016383212244\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The isolation and preliminary characterization of a trypsin-like protease with high activity at 20 degrees C is described. This protease was isolated from Antarctic krill (Euphasia superba) by a two-step chromatography process and the use of zymogram analyses. The protease has a molecular weight of 30 kDa and a pI of 4.1. Its specific activity at 20 degrees C on BAPNA is 0.5 U/mg.</p>\",\"PeriodicalId\":9179,\"journal\":{\"name\":\"Bioseparation\",\"volume\":\"10 4-5\",\"pages\":\"237-41\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1023/a:1016383212244\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioseparation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1023/a:1016383212244\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioseparation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1023/a:1016383212244","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Isolation, purification and preliminary characterization of cryophilic proteases of marine origin.
The isolation and preliminary characterization of a trypsin-like protease with high activity at 20 degrees C is described. This protease was isolated from Antarctic krill (Euphasia superba) by a two-step chromatography process and the use of zymogram analyses. The protease has a molecular weight of 30 kDa and a pI of 4.1. Its specific activity at 20 degrees C on BAPNA is 0.5 U/mg.
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