Differences in C‐terminal amino acid sequences between erythrocyte and liver cytochrome b5 isolated from pig and human
- 24 April 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 169 (2) , 143-146
- https://doi.org/10.1016/0014-5793(84)80306-3
Abstract
Two forms of cytochrome b 5, a soluble erythrocyte form and a membrane‐bound liver form, were purified from pig and human, and structural differences between them were analyzed. Porcine and human erythrocyte cytochrome b 5 consisted of 97 amino acid residues and contained the same catalytic domain structure (residue 1–96) as that of the corresponding liver cytochrome b 5, but had one amino acid replacement at the C‐terminus (residue 97). These results suggest that erythrocyte cytochrome b 5 is not derived from the liver protein by proteolysis but a translational product from another distinct mRNA of cytochrome b 5.Keywords
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