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Purification and partial characterization of cytochrome c<sub>552</sub> from Halobacterium salinarium
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View Archive Info| Field | Value | |
| Title |
Purification and partial characterization of cytochrome c552 from Halobacterium salinarium
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| Creator |
Sreeramulu, K
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| Subject |
Cytochrome c552
Halobacterium salinarium purification characterization |
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| Description |
274-277
Cytochrome 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. |
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| Date |
2009-04-13T10:00:56Z
2009-04-13T10:00:56Z 2003-08 |
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| Type |
Article
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| Identifier |
0301-1208
http://hdl.handle.net/123456789/3802 |
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| Language |
en_US
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| Publisher |
CSIR
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| Source |
IJBB Vol.40(4) [August 2003]
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