Controlled Proteolysis of Flavocytochrome b2. Characterization of a 15000-Dalton Heme-Binding Core and Comparison with Detergent Solubilized Cytochrome b5
نویسندگان
چکیده
منابع مشابه
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In earlier work (2, 3) the isolation, physical properties, and chemical reactions of rabbit liver microsomal cytochrome bs were described. The nature of heme’ binding in this heme protein has now been examined with calf liver microsomal cytochrome bs. This first involved the preparation of undenatured apocytochrome b5 and the apoprotein of an iodinated and acetylated derivative of cytochrome b5...
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Isolation and characterization of the cytochrome domain of flavocytochrome b2 expressed independently in Escherichia coli.
The cytochrome domain of flavocytochrome b2 (L-lactate dehydrogenase) was expressed in the bacterium Escherichia coli and a purification procedure was developed. When expressed in E. coli, the b2-cytochrome domain contains protohaem IX and has an electronic absorption spectrum identical with that of the cytochrome b2 'core' produced by proteolytic cleavage of the enzyme isolated from yeast. The...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1976
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1976.tb10828.x