Knecht E, Roche E
FEBS Lett. 1986 Oct 6;206(2):339-42. doi: 10.1016/0014-5793(86)81008-0.
NADH and NADPH accelerate the 'in vitro' rate of proteolysis of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by elastase and other proteases, including lysosomal proteases. NAD+ and NADP+ have the opposite effect. Since there is a good correlation between proteolytic susceptibility of proteins and their 'in vivo' degradation rates, a possible role of the reduction-oxidation status in controlling the intracellular degradation of GAPDH is advanced.
NADH和NADPH可加速3-磷酸甘油醛脱氢酶（GAPDH）在体外被弹性蛋白酶及包括溶酶体蛋白酶在内的其他蛋白酶的蛋白水解速率。NAD+和NADP+则有相反作用。鉴于蛋白质的蛋白水解敏感性与其体内降解速率之间存在良好的相关性，因此提出了还原-氧化状态在控制GAPDH细胞内降解中可能发挥的作用。
