Abstract
Two kinds of acidic arginine amidase activity were found in boar sperm. One enzyme was separated by a treatment consisting of lima bean trypsin inhibitor (LBTI) affinity adsorption and elution. The other enzyme was separated by aprotinin affinity adsorption and elution through the same solutions as those used for first enzyme; the two enzymes provisionally named boar sperm acidic arginine amidases 1 (BSAA-1) and 2 (BSAA-2), respectively. The amidolytic activity of BSAA-1 was increased by high concentrations of calcium chloride, while the activity of BSAA-2 was independent of calcium chloride. Their behavior with LBTI and aprotinin, and profiles of their substrate specificities, were also different. The affinity of LBTI to BSAA-1 was approximately 14 times higher than that to BSAA-2.
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