Biochemical studies on the muscle microsomes of Ascaris lumbricoides var. suum. II. Purification and characterization of b-type cytochrome and NADH-ferricyanide reductase from Ascaris muscle microsomes.:II. Purification and Characterization of b-Type Cytochrome and NADH-Ferricyanide Reductase form <i>Ascaris</i> Muscle Microsomes

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  • MATUDA Sadayuki
    Department of Biochemistry, Faculty of Medicine, Kagoshima University

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Description

A b-type cytochrome and NADH-ferricyanide (FC) reductase were solubilized from Ascaris muscle microsomes by detergents and purified by column chromatography.<br> 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.<br> 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.<br> 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.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 85 (2), 351-358, 1979

    The Japanese Biochemical Society

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