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PARTIAL CHARACTERIZATION OF A NEW BULL SPERM ARYLAMIDASE

Enzymes which hydrolyse the amide linkage of aminoacyl napthylamides, are generally called arylamidases, napthylamidases or arylaminopeptidases. Such enzymes are found in many tissues and organisms and may exhibit specificity for certain acidic, basic and/or neutral amino acid-β-naphthylamides. Some arylamidases are exopeptidases or endopeptidases. The present report describes the partial characterization of a new bull sperm arylamidase which exhibited a greater relative rate of hydrolysis with L-methionyl-β-naphthylamide than with ten other amino acid naphthylamides. Preliminary aspects of this work were briefly reported elsewhere (Meizel & Cotham, 1971).

Assays of enzymatic activity during and after purification of the enzyme were based on the spectrofluorometric detection of the β-naphthylamine released during enzymatic hydrolysis of the amino acid naphthylamide substrates (Greenberg, 1962). A Hitachi-Perkin-Elmer MPF-2A spectrofluorometer was utilized for these assays