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Differences in C‐terminal amino acid sequences between erythrocyte and liver cytochrome b 5 isolated from pig and human
Author(s) -
Kimura Sadao,
Abe Kiyoshi,
Sugita Yoshiki
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80306-3
Subject(s) - cytochrome b5 , biochemistry , cytochrome c , cytochrome , cytochrome b , proteolysis , pig liver , residue (chemistry) , amino acid residue , hemeprotein , chemistry , peptide sequence , amino acid , biology , heme , mitochondrion , enzyme , gene , mitochondrial dna
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 .