Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes.

作者: Toshitsugu YUBISUI , Toshiyuki MIYATA , Sadaaki IWANAGA , Minoru TAMURA , Satoshi YOSHIDA

DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A134871

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摘要: 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 a deficiency this enzyme. protein is hydrophilic whole, but two regions, Phe-36 Ile-71 and Met-231 Phe-275, were found be highly hydrophobic. latter region particularly unique, rich in proline (20%). amino-terminal very similar partial sequences corresponding regions enzymes pig steer liver microsomes.

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