A partial purification of membrane-bound b and c cytochromes from Chromatium vinosum

Knaff, David B.; Worthington, Thomas M.; White, Craig C.; Malkin, Richard

doi:10.1016/0003-9861(79)90081-x

Cited by 8 publications

(1 citation statement)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Knaff and Buchanan suggested the presence of the b-type cytochrome in Chromatium chromatophores (8), and later Knaff et al made the characterization of a partially purified membrane-bound b-cytochrome (9). They obtained a preparation containing b-type cytochrome (b-560) by treatment of chromatophores with deoxycholate followed by ammonium sulfate fractionation and 132 gel filtration on Bio-Gel A 1.5.…”

Section: Introductionmentioning

confidence: 99%

Isolation and purification of membrane-bound cytochrome b-560 from photosynthetic bacterium Chromatium vinosum

1982

View full text Add to dashboard Cite

A membrane-bound cytochrome of the b-type (cytochrome b-560) was success-fully purified from chromatophores of the photosynthetic purple sulfur bacterium Chromatium vinosum by treatment with sodium cholate, sodium deoxycholate, sodium thiocyanate, and bacterial alkaline protease (EC 3·4·21·14) followed by gel filtration.The purified cytochrome b-560 showed the absorption maxima at 279, 412.5 and 533 nm in the oxidized form, and 427, 530 and 560 nm in the reduced form. Reduced-minus-oxidized difference millimolar absorption coefficient was 14.0 for a wavelength pair, 560 minus 540 nm.Isolated cytochrome b-560 was electrophoretically homogeneous, and its minimal molecular weight was estimated to the 13,000 by SDS polyacrylamide gel electrophoresis.The midpoint potential at pH 8.0 was -110mV, and was not dependent on the ambient pH in the pH range of 6.8 to 8.8.

show abstract

Section: Introductionmentioning

confidence: 99%