Molecular properties of succinate dehydrogenase isolated from Micrococcus luteus (lysodeikticus).

Journal of Bacteriology
B A Crowe, P Owen

Abstract

Succinate dehydrogenase (EC 1.3.99.1) of Micrococcus luteus was selectively precipitated from Triton X-100-solubilized membranes by using specific antiserum. The precipitated enzyme contained equimolar amounts of four polypeptides with apparent molecular weights of 72,000, 30,000, 17,000, and 15,000. The 72,000 polypeptide possessed a covalently bound flavin prosthetic group and appeared to be strongly antigenic as judged by immunoprinting experiments. Low-temperature absorption spectroscopy revealed the presence of cytochrome b556 in the antigen complex. By analogy with succinate dehydrogenase purified from other sources, the 72,000 and 30,000 polypeptides were considered to represent subunits of the succinate dehydrogenase enzyme, whereas one (or both) of the low-molecular-weight polypeptides was attributed to the apoprotein of the b-type cytochrome. A succinate dehydrogenase antigen cross-reacting with the M. luteus enzyme complex could be demonstrated in membranes of Micrococcus roseus, Micrococcus flavus, and Sarcina lutea, but not in the membranes isolated from a wide variety of other gram-positive and gram-negative bacteria.

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Jul 1, 1950·Journal of Bacteriology·B D DAVIS, E S MINGIOLI

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Citations

May 28, 2004·Microbial Ecology·C L GreenblattR J Cano
Jan 29, 2000·Protein Expression and Purification·D J ClarkD J Opheim
Sep 14, 1988·Biochimica Et Biophysica Acta·J D PennoyerB L Trumpower
Sep 1, 1987·Archives of Biochemistry and Biophysics·V ArtzatbanovA Azzi

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