Geoffrey W. Krissansen, Clive N.A. Trotman, Warren P. Tate
{"title":"一种新的蛋白酶可以解释盐蒿血红蛋白结构的广泛不同模型","authors":"Geoffrey W. Krissansen, Clive N.A. Trotman, Warren P. Tate","doi":"10.1016/0005-2795(81)90100-8","DOIUrl":null,"url":null,"abstract":"<div><p>Evidence that a protease is responsible for the proposal of differing models for the structure of the haemoglobin of the brine shrimp <em>Artemia salina</em> is presented. The protease, a minor contaminant in highly purified haemoglobin preparations, is activated by SDS of the SDS-polyacrylamide gel system and readily degrades the haemoglobin subunit. Removal of the protease by chromatography on Con A-Sepharose 4B has shown the haemoglobin (<span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub><mtext> 260 000</mtext></math></span>) to comprise two subunits of <span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub><mtext> 130 000</mtext></math></span>.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 104-108"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90100-8","citationCount":"14","resultStr":"{\"title\":\"A novel protease may explain widely differing models for the structure of Artemia salina haemoglobin\",\"authors\":\"Geoffrey W. Krissansen, Clive N.A. Trotman, Warren P. Tate\",\"doi\":\"10.1016/0005-2795(81)90100-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Evidence that a protease is responsible for the proposal of differing models for the structure of the haemoglobin of the brine shrimp <em>Artemia salina</em> is presented. The protease, a minor contaminant in highly purified haemoglobin preparations, is activated by SDS of the SDS-polyacrylamide gel system and readily degrades the haemoglobin subunit. Removal of the protease by chromatography on Con A-Sepharose 4B has shown the haemoglobin (<span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub><mtext> 260 000</mtext></math></span>) to comprise two subunits of <span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub><mtext> 130 000</mtext></math></span>.</p></div>\",\"PeriodicalId\":100165,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"volume\":\"671 1\",\"pages\":\"Pages 104-108\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-11-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2795(81)90100-8\",\"citationCount\":\"14\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005279581901008\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581901008","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A novel protease may explain widely differing models for the structure of Artemia salina haemoglobin
Evidence that a protease is responsible for the proposal of differing models for the structure of the haemoglobin of the brine shrimp Artemia salina is presented. The protease, a minor contaminant in highly purified haemoglobin preparations, is activated by SDS of the SDS-polyacrylamide gel system and readily degrades the haemoglobin subunit. Removal of the protease by chromatography on Con A-Sepharose 4B has shown the haemoglobin () to comprise two subunits of .