1979 Volume 85 Issue 2 Pages 351-358
A b-type cytochrome and NADH-ferricyanide (FC) reductase were solubilized from Ascaris muscle microsomes by detergents and purified by column chromatography.
The purified b-type cytochrome displayed absorption bands at 560 (α-peak), 525 (β-peak), and 424nm (γ-peak), with a marked shoulder at 555nm in the reduced form, 415nm (γ-peak) in the oxidized form. This absorption spectrum was different from that of rat liver microsomal cytochrome b5.
The molecular weight was estimated to be about 100, 000 by SDS-polyacrylamide gel electrophoresis, and the absorption spectrum of alkaline pyridine ferrohemochrome suggested that the prosthetic group of this cytochrome is protoheme.
The molecular weight of the purified NADH-FC reductase was estimated to be about 55, 000 by SDS-polyacrylamide gel electrophoresis. The purified reductase required NADH as a specific electron donor. The reductase efficiently reduced some redox dyes with NADH, but the reduction of cytochrome c was much slower. The purified reductase, like the mem-brane-bound reductase, was not inhibited by thiol reagents.
