Purification and partial characterization of cytochrome c552 from Halobacterium salinarium.
Cytochrome c552 was purified to near homogenity and partially characterized from Halobacterium salinarium JWS mutant, devoid of carotenoid pigments. The purification involved the extraction of membranes with 1% Triton X-100, followed by butylagarose, DEAE-Sepharose CL6B and hydroxyapatite column chromatography. The fold of purification was 16. The purified cytochrome showed maximum absorption at 552 nm. The molecular mass determined by SDS-PAGE was found to be 14.1 kD.
Department of Biochemistry, Gulbarga University Gulbarga-585 106, Karnataka, India. ksramu@rediffmail.com
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Sreeramulu
D003574:Cytochrome c Group / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D019617:Halobacterium salinarum / Q000201:enzymology*; D007700:Kinetics; D010084:Oxidation-Reduction
D003574:Cytochrome c Group; C022302:cytochrome C-552