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- W1910107413 abstract "Subunit d of H+-ATP synthase from rat liver mitochondria was isolated from the purified enzyme by reverse-phase high performance liquid chromatography. The partial amino acid sequence of the subunit was determined by automated Edman degradation of the peptide fragments. The nucleotide sequence of subunit d of rat liver H+-ATP synthase was determined from a recombinant cDNA clone isolated by screening a rat hepatoma cell line H4TG cDNA library with a probe DNA. The sequence was composed of 581 nucleotides including a coding region for the import precursor of subunit d and noncoding regions on the 5- and 3' -sides. The possible precursor of subunit d and its mature polypeptide deduced from the open reading frame consisted of 161 and.160 amino acid residues with molecular weights of 18, 763 and 18, 631, respectively. Subunit d is a hydrophilic protein with an isoelectric point of 6.19. The sequence of the rat subunit d is highly homologous with that of subunit d of bovine heart and slightly similar to that of the subunit d of the yeast mitochondria. However, it had no homology with the sequence of any of the subunits of bacterial or chloroplast H+-ATP synthase." @default.
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- W1910107413 date "1993-11-01" @default.
- W1910107413 modified "2023-09-27" @default.
- W1910107413 title "The Complete Amino Acid Sequence of Subunit d of Rat Liver Mitochondrial H+-ATP Synthase1" @default.
- W1910107413 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a124242" @default.
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