title: [Mechanism of interaction of pyridoxal-5-phosphate with human serum albumin].
abstract: Four and five molecules of pyridoxal-5-phosphate are irreversibly bound to human serum albumin in neutral aqueous or aqueous-spirituous media, respectively. The first step is a reversible formation of the Schiff bases with lysine residues. It is followed by an irreversible interaction of aldimine bond with an imidazole ring of the neighbouring histidine to form cyclic compounds of substituted aldimine type. Cyclic products of the reaction are characterized by absorption spectra with a maximum at 330 nm and fluorescence spectra with a maximum at 400-410 nm in a neutral medium.
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D005453:Fluorescence; D006801:Humans; D006868:Hydrolysis; D011732:Pyridoxal Phosphate; D012709:Serum Albumin
chemical_list: D012709:Serum Albumin; D011732:Pyridoxal Phosphate
vernacular_title: Mekhanizm vzaimodeĭstviia piridoksal'-5-fosfata s syvorotochnym al'buminom cheloveka.