{"title":"Calosoma calum (FAB.)和Carabus teedatus FAB中胰蛋白酶的研究","authors":"A.C Cheung, R.H Gooding","doi":"10.1016/0010-406X(70)90561-X","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. By use of specific synthetic substrates and inhibitors, trypsin and chymotrypsin have been demonstrated in the digestive tracts of both sexes of adult <em>Carabus taedatus</em> and <em>Calosoma calidum</em>.</p></span></li><li><span>2.</span><span><p>2. No evidence for carboxypeptidase-A, carboxypeptides-B or aminopeptidase was found.</p></span></li><li><span>3.</span><span><p>3. At 30°C the trypsin has a pH optimum at pH 8·2–8·3.</p></span></li><li><span>4.</span><span><p>4. The trypsin has been partially purified and its molecular weight estimated by Sephadex G-100 column chromatography to be approximately 20,000–23,000.</p></span></li><li><span>5.</span><span><p>5. The trypsin is inhibited by TLCK, PMSF, 2-mercapto-ethanol, human and porcine serum.</p></span></li></ul></div>","PeriodicalId":78189,"journal":{"name":"Comparative biochemistry and physiology","volume":"37 3","pages":"Pages 331-338"},"PeriodicalIF":0.0000,"publicationDate":"1970-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0010-406X(70)90561-X","citationCount":"15","resultStr":"{\"title\":\"A study of trypsin in Calosoma calidum (FAB.) and Carabus taedatus FAB\",\"authors\":\"A.C Cheung, R.H Gooding\",\"doi\":\"10.1016/0010-406X(70)90561-X\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. By use of specific synthetic substrates and inhibitors, trypsin and chymotrypsin have been demonstrated in the digestive tracts of both sexes of adult <em>Carabus taedatus</em> and <em>Calosoma calidum</em>.</p></span></li><li><span>2.</span><span><p>2. No evidence for carboxypeptidase-A, carboxypeptides-B or aminopeptidase was found.</p></span></li><li><span>3.</span><span><p>3. At 30°C the trypsin has a pH optimum at pH 8·2–8·3.</p></span></li><li><span>4.</span><span><p>4. The trypsin has been partially purified and its molecular weight estimated by Sephadex G-100 column chromatography to be approximately 20,000–23,000.</p></span></li><li><span>5.</span><span><p>5. The trypsin is inhibited by TLCK, PMSF, 2-mercapto-ethanol, human and porcine serum.</p></span></li></ul></div>\",\"PeriodicalId\":78189,\"journal\":{\"name\":\"Comparative biochemistry and physiology\",\"volume\":\"37 3\",\"pages\":\"Pages 331-338\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1970-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0010-406X(70)90561-X\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative biochemistry and physiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0010406X7090561X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative biochemistry and physiology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0010406X7090561X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A study of trypsin in Calosoma calidum (FAB.) and Carabus taedatus FAB
1.
1. By use of specific synthetic substrates and inhibitors, trypsin and chymotrypsin have been demonstrated in the digestive tracts of both sexes of adult Carabus taedatus and Calosoma calidum.
2.
2. No evidence for carboxypeptidase-A, carboxypeptides-B or aminopeptidase was found.
3.
3. At 30°C the trypsin has a pH optimum at pH 8·2–8·3.
4.
4. The trypsin has been partially purified and its molecular weight estimated by Sephadex G-100 column chromatography to be approximately 20,000–23,000.
5.
5. The trypsin is inhibited by TLCK, PMSF, 2-mercapto-ethanol, human and porcine serum.
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