{"title":"人、牛、兔纤溶酶原含色氨酸位点随溶液ph值变化的状态","authors":"V.N. Nikandrov, G.V. Vorobyova, N.V. Demidchik","doi":"10.1016/0020-711X(94)90076-0","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The state of tryptophan-containing sites is proved to be stable by intrinsic tryptophan fluorescence with pH 5–8, 7–9, and 6–9 in human, rabbit and bovine plasminogen molecules, respectively.</p></span></li><li><span>2.</span><span><p>2. With pH < 5.0 tryptophan-containing sites of human zymogen (in contrast to rabbit and bovine ones) undergo conformational transitions.</p></span></li><li><span>3.</span><span><p>3. With the shift of solution pH from 9 to 12 tryptophan-containing sites of human and rabbit plasminogens are partially disorganized, while tryptophanyls become more available for solvent.</p></span></li><li><span>4.</span><span><p>4. Tryptophan-containing sites of bovine plasminogen molecules are less mobile in structure during changes of solution pH.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 1043-1047"},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90076-0","citationCount":"1","resultStr":"{\"title\":\"The state of tryptophan-containing sites of human, bovine and rabbit plasminogens with changing solution pHs\",\"authors\":\"V.N. Nikandrov, G.V. Vorobyova, N.V. Demidchik\",\"doi\":\"10.1016/0020-711X(94)90076-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The state of tryptophan-containing sites is proved to be stable by intrinsic tryptophan fluorescence with pH 5–8, 7–9, and 6–9 in human, rabbit and bovine plasminogen molecules, respectively.</p></span></li><li><span>2.</span><span><p>2. With pH < 5.0 tryptophan-containing sites of human zymogen (in contrast to rabbit and bovine ones) undergo conformational transitions.</p></span></li><li><span>3.</span><span><p>3. With the shift of solution pH from 9 to 12 tryptophan-containing sites of human and rabbit plasminogens are partially disorganized, while tryptophanyls become more available for solvent.</p></span></li><li><span>4.</span><span><p>4. Tryptophan-containing sites of bovine plasminogen molecules are less mobile in structure during changes of solution pH.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 8\",\"pages\":\"Pages 1043-1047\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90076-0\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94900760\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94900760","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The state of tryptophan-containing sites of human, bovine and rabbit plasminogens with changing solution pHs
1.
1. The state of tryptophan-containing sites is proved to be stable by intrinsic tryptophan fluorescence with pH 5–8, 7–9, and 6–9 in human, rabbit and bovine plasminogen molecules, respectively.
2.
2. With pH < 5.0 tryptophan-containing sites of human zymogen (in contrast to rabbit and bovine ones) undergo conformational transitions.
3.
3. With the shift of solution pH from 9 to 12 tryptophan-containing sites of human and rabbit plasminogens are partially disorganized, while tryptophanyls become more available for solvent.
4.
4. Tryptophan-containing sites of bovine plasminogen molecules are less mobile in structure during changes of solution pH.
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