Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes.
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Yubisui T, Miyata T, Iwanaga S, Tamura M, Yoshida S, Takeshita M, Nakajima H
Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes.
J Biochem. 1984 Aug;96(2):579-82.
- PubMed ID
- 6389526 [ View in PubMed]
- 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.