Purification and properties of the soluble NAD glycohydrolase from Bungarus fasciatus venom.
作者： D.A. Yost , B.M. Anderson
DOI: 10.1016/S0021-9258(19)69502-5
关键词:
摘要: The NAD glycohydrolase (NADase) (EC 3.2.2.5) from Bungarus fasciatus (banded krait) venom was purified (1000-fold) to electrophoretic homogeneity through a 3-step purification procedure, the last step being affinity chromatography on Cibacron blue agarose. NADase is glycoprotein containing two subunits of Mr = 62,000 each. Nicotinamide and adenosine diphosphoribose were produced in 1:1 stoichiometry only products formed when incubated with NAD. These results confirmed by high performance liquid chromatography. enzyme exhibited brod pH profile optimum for hydrolysis at 7.5 very little change Km 6.0 8.5. slightly affected changes ionic strength. studied titrimetrically 38 degrees C 14 microM Vmax 1380 mumol cleaved/min/mg protein. activation energy enzyme-catalyzed 15.7 kcal/mol. In addition NADP, number analogs shown function as substrates enzyme. Product inhibition studies demonstrated nicotinamide be noncompetitive inhibitor KI 1.5 mM competitive 0.36 mM. Procion HB (Cibacron F3GA) 33 nmol. catalyzed pyridine base exchange reaction between 3-acetylpyridine moiety
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