NAD glycohydrolase(NADase) tightly bound to rabiit erythrocyte membranes was solubilized and its properties were characterized.
The membrane-bound NADase was slightly solubilized with 1% Triton X-100 or 1M KCL, but completely solubiilzed with 1% Trito...
NAD glycohydrolase(NADase) tightly bound to rabiit erythrocyte membranes was solubilized and its properties were characterized.
The membrane-bound NADase was slightly solubilized with 1% Triton X-100 or 1M KCL, but completely solubiilzed with 1% Triton X-100-1M KCL solution.
The solubilized enzyme hydrolyzed β-NAD with Km of 0.39mM and NADP with Km of 1.98mM, but did not hydrolyzed α-NAD and NMN. Urea activated the hydrolysis of NAD and NADP with the same rate of 3-fold by the solubilized membrane fraction, suggesting that the hydrolysis of NAD and NADP is catalyzed by the same enzyme, NAD glycohydrolase.
The molecular weight of rabbit erythrocyte membrane NADase determined by Sephadex G-150 gel filtration wat about 170,000 daltons.