Interactions of pyridoxal kinase and aspartate aminotransferase emission anisotropy and compartmentation studies.
作者： Y T Kim , F Kwok , J E Churchich
DOI: 10.1016/S0021-9258(18)68299-7
关键词: Dissociation constant 、 Pyridoxal kinase 、 Alkaline phosphatase 、 Phosphorylation 、 Enzyme 、 Cofactor 、 Kinase 、 Biochemistry 、 Chemistry 、 Affinity chromatography
摘要: Abstract Physical interactions between pyridoxal kinase and aspartate aminotransferase were detected by means of emission anisotropy affinity chromatography techniques. Binding (apoenzymes) to tagged with a fluorescent probe was measurements at pH 6.8 (150 mM KCl). Upon saturation the aminotransferase, increases 22%. The protein complex is characterized dissociation constant 3 microM. Time-dependent conducted mixture 5-naphthylamine-1-sulfonic acid-kinase (apoenzyme), revealed presence two rotational correlation times phi 1 = 36 2 62 ns. longer time attributed stable complex. By immobilizing one enzyme (pyridoxal kinase) through pyridoxal-Sepharose, it possible demonstrate that releases kinase. A test compartmentation pyridoxal-5-phosphate within using alkaline phosphatase as trapping agent, indicates cofactor generated catalytic action channeled apotransaminase. main function formed hinder release free into bulk solvent.
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