title: The primary structure of pig liver thioltransferase.
abstract: The complete amino acid sequence of pig liver thioltransferase has been determined. The homogeneous protein was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The resulting peptides were purified by reversed-phase high performance liquid chromatography and ion-exchange fast protein liquid chromatography. Sequencing of the fragments was achieved with either automated Edman degradation or fast atom bombardment-mass spectrometry. Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus. The protein has 2 cysteine pairs with sequences of -Cys-Pro-Phe-Cys- and -Cys-Ile-Gly-Gly-Cys-, the first pair of which (Cys22 and Cys25) is located at the potential active site of the enzyme. The sequence of pig liver thioltransferase displays close homology (82%) with calf thymus glutaredoxin, suggesting that they belong to the same evolutionary family.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D054477:Glutaredoxins; D008099:Liver / Q000201:enzymology*; D013058:Mass Spectrometry; D010088:Oxidoreductases; D010446:Peptide Fragments / Q000032:analysis; D011490:Protein Disulfide Reductase (Glutathione); D013552:Swine; D014357:Trypsin
chemical_list: D054477:Glutaredoxins; D010446:Peptide Fragments; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione); D014357:Trypsin