{"title":"Tris-HCl是否有效参与血红蛋白吡哆基化过程中的转氨化?","authors":"P Menu, C Geschier, C Vigneron, P Labrude","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>To test whether Tris is required for covalent binding of pyridoxal phosphate (PLP) to hemoglobin, we carried out the reaction in solutions of Tris homologues, carrying a blocked amine function. With the exception of Mono-Tris, these compounds permitted the synthesis of modified hemoglobins with acceptable spectral properties, P50 values, cooperativity and methemoglobin content, refuting Tris HCI participation during hemoglobin pyridoxylation.</p>","PeriodicalId":8948,"journal":{"name":"Biomedica biochimica acta","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Does Tris-HCl effectively participate in transamination during hemoglobin pyridoxylation?\",\"authors\":\"P Menu, C Geschier, C Vigneron, P Labrude\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>To test whether Tris is required for covalent binding of pyridoxal phosphate (PLP) to hemoglobin, we carried out the reaction in solutions of Tris homologues, carrying a blocked amine function. With the exception of Mono-Tris, these compounds permitted the synthesis of modified hemoglobins with acceptable spectral properties, P50 values, cooperativity and methemoglobin content, refuting Tris HCI participation during hemoglobin pyridoxylation.</p>\",\"PeriodicalId\":8948,\"journal\":{\"name\":\"Biomedica biochimica acta\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomedica biochimica acta\",\"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":"Biomedica biochimica acta","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Does Tris-HCl effectively participate in transamination during hemoglobin pyridoxylation?
To test whether Tris is required for covalent binding of pyridoxal phosphate (PLP) to hemoglobin, we carried out the reaction in solutions of Tris homologues, carrying a blocked amine function. With the exception of Mono-Tris, these compounds permitted the synthesis of modified hemoglobins with acceptable spectral properties, P50 values, cooperativity and methemoglobin content, refuting Tris HCI participation during hemoglobin pyridoxylation.
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