Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3802
Title: Purification and partial characterization of cytochrome c<sub>552</sub> from Halobacterium salinarium
Authors: Sreeramulu, K
Keywords: Cytochrome c<sub>552</sub>
Halobacterium salinarium
purification
characterization
Issue Date: Aug-2003
Publisher: CSIR
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.
Description: 274-277
URI: http://hdl.handle.net/123456789/3802
ISSN: 0301-1208
Appears in Collections:IJBB Vol.40(4) [August 2003]

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