منابع مشابه
Synthesis of rat liver microsomal cytochrome b5 by free ribosomes
Free and membrane-bound polyribosomes were separated from liver homogenates and characterized by electron microscopy. Using the wheat germ cell-free translation system, total translation products of poly A+RNA extracted from free polyribosomes (poly A+RNAf) showed some correlation to total liver cytosol proteins. In contrast, translation products of poly A+RNA from membrane-bound polyribosomes ...
متن کاملAmino acid sequence of rabbit liver microsomal cytochrome b5.
Cytochrome bs from the rabbit liver microsomes was solubilized with pancreatic lipase. The apoprotein of the predominant form of cytochrome bs was hydrolyzed with trypsin and chymotrypsin and the resulting peptides were isolated. The complete amino acid sequences of these peptides were determined by the Edman degradation procedure. For the first 90 residues, this amino acid sequence is essentia...
متن کاملThe nature of the heme binding in microsomal cytochrome b5.
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...
متن کاملNADH cytochrome b5 reductase and cytochrome b5 catalyze the microsomal reduction of xenobiotic hydroxylamines and amidoximes in humans.
Hydroxylamine metabolites, implicated in dose-dependent and idiosyncratic toxicity from arylamine drugs, and amidoximes, used as pro-drugs, are metabolized by an as yet incompletely characterized NADH-dependent microsomal reductase system. We hypothesized that NADH cytochrome b5 reductase and cytochrome b5 were responsible for this enzymatic activity in humans. Purified human soluble NADH cytoc...
متن کاملHomology between bakers' yeast cytochrome b2 and liver microsomal cytochrome b5.
The amino-acid sequence of the hemebinding region of bakers' yeast cytochrome b(2) [L-(+)-lactate dehydrogenase, EC 1.1.2.3] has been determined. It shows a strong similarity with the sequence of microsomal cytochrome b(5), and appears to be compatible with the same kind of peptide-chain folding, in agreement with data obtained previously by various physiochemical methods. The comparison shows ...
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ژورنال
عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology
سال: 2018
ISSN: 1768-3262
DOI: 10.4267/2042/66058