PURIFICATION AND PROPERTIES OF A MEMBRANE-BOUND NADH-CYTOCHROME-B5 REDUCTASE FROM ERYTHROCYTES OF THE SIPUNCULID WORM, PHASCOLOPSIS-GOULDII
PURIFICATION AND PROPERTIES OF A MEMBRANE-BOUND NADH-CYTOCHROME-B5 REDUCTASE FROM ERYTHROCYTES OF THE SIPUNCULID WORM, PHASCOLOPSIS-GOULDII
复制标题
DOI：
10.1016/0167-4838(89)90211-2
复制
发表时间：
1989-11-30
期刊：
影响因子：
--
通讯作者：
KURTZ, DM
中科院分区：
文献类型：
--
作者：
BONOMI, F;LONG, RC;KURTZ, DM
The purification to homogeneity of the membrane-bound NADH-cytochrome-b5 reductase from erythrocytes of the sipunculid, Phascolopsis gouldii is reported. This highly purified reductase has allowed more detailed characterizations of its molecular and kinetic properties than was possible in a previous study (Utecht, R.E. and Kurtz, D.M., Jr. (1988) Biochim. Biophys. Acta 953, 164-178). The reductase has a molecular weight of 34,000 and contains FAD as the prosthetic group. In aqueous solution containing 0.5 vol% Triton X-100, the reductase forms an aggregate of Mr .apprx. 220,000. A higher purity preparation of P. gouldii erythrocyte cytochrome b5 was also obtained. The combination of purified, solubilized reductase and cytochrome b5 was shown to catalyze the quantitative two-electron reduction of [Fe(III),Fe(III)]methemerythrin to [Fe(II),Fe(II)]deoxyhemerythrin by NADH. The P. gouldii NADH-cytochrome b5 reductase is the first hemerythrin-containing erythrocytes to be purified and characterized. This methemerythrin reduction system appears to be analogous to methemoglobin reductases from vertebrate erythrocytes.
