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Isolation and properties of membrane-bound cytochromec-552 from photosynthetic bacteriumChromatium vinosum

โœ Scribed by Michio Doi; Ken -Ichiro Takamiya; Mitsuo Nishimura


Book ID
104619574
Publisher
Springer
Year
1983
Tongue
English
Weight
569 KB
Volume
4
Category
Article
ISSN
0166-8595

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โœฆ Synopsis


A membrane-bound cytochrome c-552 was isolated and purified from the photosynthetic bacterium Chromatium vinosum by treatment with sodium cholate, sodium deoxycholate and bacterial alkaline protease followed by gel filtration.

The purified cytochrome c-552, which may have been modified by the protease treatment, was electrophoretically homogeneous. Its minimal molecular weight was estimated to be 19 and 20 kdaltons, respectively by SDS polyacrylamide gel electrophoresis and by gel filtration on Sephadex G-100.

Cytochrome c-552 showed the absorption maxima at 419, 523 and 552 nm in the reduced form. Reduced-minus-oxidized difference millimolar absorption coefficient was 10.6 for the wavelength pair, 552 minus 540nm. The midpoint potential at pH8.0 was --130 mV. The polarity in the amino acid composition of cytochrome c-552 was 40.1% and reflected its hydrophobicity.

The solubilized cytochrome c-552 was shown to be a different entity from the soluble flavocytochrome c-552 in several respects.


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