Differences in C‐terminal amino acid sequences between erythrocyte and liver cytochrome b 5 isolated from pig and human

FEBS Letters

Kimura, Sadao²  Sugita, Yoshiki²  Abe, Kiyoshi¹ 

[1] Tsukuba University College of Medical Technology and Nursing, Sakura, Niihari, Ibaraki 305, Japan;Department of Biochemistry, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba, Japan

关键词: Liver;    Erythrocyte;    Cytochrome b 5;    Amino acid sequence;    Protein homology;    HPLC;   

DOI  :  10.1016/0014-5793(84)80306-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown