Abstract
Tripeptide aminopeptidase (EC 3.4.11.4) was purified from bovine dental follicles by a series of chromatographies. Purified enzyme had a specific activity of 59.5 units per mg protein with L-prolyl-glycylglycine as substrate. The pH optimum was 8.0. The purified native enzyme had a Mr of 230,000 and was shown to be a tetramer of subunit Mr of 58,000. The isoelectric point was pH 7.0. The enzyme was inhibited 5-5′-dithio-bis (2-nitrobenzoic acid),o-phenanthroline, and bestatin. Substrate specificity studies indicated that the enzyme specifically hydrolyzes the N-terminal amino acid residue from tripeptides only.
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Hiraoka, B.Y., Harada, M. Purification and characterization of tripeptide aminopeptidase from bovine dental follicles. Mol Cell Biochem 129, 87–92 (1993). https://doi.org/10.1007/BF00926579
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DOI: https://doi.org/10.1007/BF00926579