Homology Between Bakers' Yeast Cytochrome b2 and Liver Microsomal Cytochrome b5

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منابع مشابه

Homology 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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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 ...

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Amino 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...

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Cytochrome c Oxidase from Bakers’ Yeast

Purified cytochrome c oxidase from bakers’ yeast can be resolved into six polypeptide bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent molecular weights of these components are I, 42,000; II, 34,500; III, 23,000; IV, 14,000; V, 12,500; and VI, 9,500. (Although Component V actually consists of two distinct polypeptide species, it will be regarde...

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Cytochrome c Oxidase from Bakers’ Yeast

Cytochrome aa3 was purified 35to 40-fold from submitochondrial particles of commercial bakers’ yeast. The purification procedure involved solubilization of the enzyme with cholate, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose in the presence of Triton x-100. The purified, active enzyme contained approximately 10 nmoles of heme a per mg of protein and was free of oth...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1974

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.71.6.2539