Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes.
The amino acid sequence of soluble NADH-cytochrome b5 reductase purified from normal human erythrocytes was determined as one approach to understand the hereditary disease of a deficiency of this enzyme. The protein is hydrophilic as a whole, but two regions, from Phe-36 to Ile-71 and from Met-231 to Phe-275, were found to be highly hydrophobic. The sequence of the latter region is particularly unique, and rich in proline (20%). The sequence of the amino-terminal region was very similar to the partial sequences of the corresponding regions of the enzymes from pig and steer liver microsomes.
D000595:Amino Acid Sequence; D003488:Cyanogen Bromide; D003579:Cytochrome Reductases / Q000097:blood* / Q000302:isolation & purification; D042966:Cytochrome-B(5) Reductase; D010450:Endopeptidases; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis
D010446:Peptide Fragments; D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase; D010450:Endopeptidases; D003488:Cyanogen Bromide