Demonstration that bovine erythrocyte cytochrome b5 is the hydrophilic segment of liver microsomal cytochrome b5
نویسندگان
چکیده
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 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 ...
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 کاملEvidence That Cytochrome b5 and Cytochrome b5 Reductase Can Act as Sole Electron Donors to the Hepatic Cytochrome P450 Systems
We previously described the development of genetic models to study the in vivo functions of the hepatic cytochrome P450 (P450) system, through the hepatic deletion of either cytochrome P450 oxidoreductase [POR; HRN (hepatic reductase null) line] or cytochrome b5 [HBN (hepatic cytochrome b5 null) line]. However, HRN mice still exhibit low levels of mono-oxygenase activity in spite of the absence...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
سال: 1982
ISSN: 0167-4838
DOI: 10.1016/0167-4838(82)90182-0