Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3802
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dc.contributor.authorSreeramulu, K-
dc.date.accessioned2009-04-13T10:00:56Z-
dc.date.available2009-04-13T10:00:56Z-
dc.date.issued2003-08-
dc.identifier.issn0301-1208-
dc.identifier.urihttp://hdl.handle.net/123456789/3802-
dc.description274-277en_US
dc.description.abstractCytochrome 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.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJBB Vol.40(4) [August 2003]en_US
dc.subjectCytochrome c552en_US
dc.subjectHalobacterium salinariumen_US
dc.subjectpurificationen_US
dc.subjectcharacterizationen_US
dc.titlePurification and partial characterization of cytochrome c552 from Halobacterium salinariumen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.40(4) [August 2003]

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