Stereospecificity of sodium borohydride reduction of Schiff bases at the active site of aspartate aminotransferase

Sodium boro[3H]hydride treatment of holoaspartate aminotransferase results in the reduction of the Schiff's base formed between pyridoxal phosphate and Lys 258. Treatment of the reduced enzyme with papain followed by acid hydrolysis liberates epsilon-N-[3H]pyridoxyl lysine which is degraded to...

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Veröffentlicht in:	The Journal of biological chemistry 1980-09, Vol.255 (18), p.8645-8649
Hauptverfasser:	Zito, S W, Martinez-Carrion, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Aspartate Aminotransferases - metabolism Binding Sites Borohydrides - pharmacology Magnetic Resonance Spectroscopy Myocardium - enzymology Protein Binding Pyridoxal Pyridoxamine Schiff Bases Swine Tritium
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