FEBS Letters | |
Differences in C‐terminal amino acid sequences between erythrocyte and liver cytochrome b 5 isolated from pig and human | |
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
【 预 览 】
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