Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5269
Title: Purification and partial characterization of cytochrome c(552) from Halobacterium salinarium
Authors: Sreeramulu, K
Keywords: cytochrome c(552)
Halobacterium salinarium
purification
characterization
Issue Date: 2003
Publisher: NATL INST SCIENCE COMMUNICATION-NISCAIR
Citation: INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS , Vol. 40 , 4 , p. 274 - 277
Abstract: Cytochrome 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.
URI: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5269
Appears in Collections:1. Journal Articles

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