title: Does Tris-HCl effectively participate in transamination during hemoglobin pyridoxylation?
abstract: 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.
authors.affiliation: Faculté des Sciences Pharmaceutiques et Biologiques, Nancy, France.
authors.forename: P
authors.initials: P
authors.lastname: Menu
authors.forename: C
authors.initials: C
authors.lastname: Geschier
authors.forename: C
authors.initials: C
authors.lastname: Vigneron
authors.forename: P
authors.initials: P
authors.lastname: Labrude
mesh_terms: D006454:Hemoglobins / Q000737:chemistry* / Q000592:standards; D006801:Humans; D011732:Pyridoxal Phosphate / Q000737:chemistry* / Q000592:standards; D012015:Reference Standards; D014325:Tromethamine
chemical_list: D006454:Hemoglobins; D014325:Tromethamine; D011732:Pyridoxal Phosphate