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. 1984 Aug;96(2):579-82.
doi: 10.1093/oxfordjournals.jbchem.a134871.

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

T Yubisui, T Miyata, S Iwanaga, M Tamura, S Yoshida, M Takeshita, H Nakajima
Free article

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

T Yubisui et al. J Biochem. 1984 Aug.
Free article

Abstract

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.

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