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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Faculté des Sciences Pharmaceutiques et Biologiques, Nancy, France.
Geschier
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Vigneron
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Labrude
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D006454:Hemoglobins / Q000737:chemistry* / Q000592:standards; D006801:Humans; D011732:Pyridoxal Phosphate / Q000737:chemistry* / Q000592:standards; D012015:Reference Standards; D014325:Tromethamine
D006454:Hemoglobins; D014325:Tromethamine; D011732:Pyridoxal Phosphate