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Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5269
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dc.contributor.authorSreeramulu, K
dc.date.accessioned2020-06-12T15:06:40Z-
dc.date.available2020-06-12T15:06:40Z-
dc.date.issued2003
dc.identifier.citationINDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS , Vol. 40 , 4 , p. 274 - 277en_US
dc.identifier.urihttp://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5269-
dc.description.abstractCytochrome C-552 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.en_US
dc.publisherNATL INST SCIENCE COMMUNICATION-NISCAIR
dc.subjectcytochrome c(552)
dc.subjectHalobacterium salinarium
dc.subjectpurification
dc.subjectcharacterization
dc.titlePurification and partial characterization of cytochrome c(552) from Halobacterium salinariumen_US
dc.typeArticle
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