A proteinase possessing the characteristics of an endopeptidase was partially purified from culture filtrates of Aeromonas proteolytica. The enzyme readily hydrolyzed hemoglobin, casein, insulin, CGPN, CGPEE, and CGP; with the latter substrate Km was 4.19 × 10−2M. Chelating agents or dialysis at low pH inhibited the proteinase, which could be reactivated under favorable conditions by the addition of certain divalent metal ions.
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Wilkes et al. (1969) studied this question.