Purification and characterization of tripeptide aminopeptidase from bovine dental follicles


Tripeptide aminopeptidase (EC 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… (More)
DOI: 10.1007/BF00926579


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