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|Title:||Purification and partial characterization of cytochrome c<sub>552</sub> from Halobacterium salinarium|
|Abstract:||Cytochrome c<sub>552</sub> 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.|
|Appears in Collections:||IJBB Vol.40(4) [August 2003]|
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