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Volumn 19, Issue 1, 2000, Pages 173-178

High-level expression in Escherichia coli and purification of the membrane-bound form of cytochrome b5

Author keywords

[No Author keywords available]

Indexed keywords

ANION EXCHANGE CHROMATOGRAPHY; APOPROTEIN; BACTERIAL MEMBRANE; BACTERIUM CULTURE; CYTOCHROME B; ENZYME PURIFICATION; ENZYME SYNTHESIS; EXPRESSION VECTOR; GEL PERMEATION CHROMATOGRAPHY; GENETIC STRAIN; HEME; ION EXCHANGE CHROMATOGRAPHY; RABBIT; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 0034043337     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1228     Document Type: Article
Times cited : (69)

References (22)
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  • 12
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    • 5 in Escherichia coli: Isolation, purification, and use of the immobilized recombinant heme protein for affinity chromatography of electron-transfer proteins
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    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J. E. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1998;289-298.
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    • Miroux, B.1    Walker, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.