A proteolytic enzyme cleaving the main component of enamel proteins obtained from immature enamel has been purified from a soluble extract of porcine immature enamel. It is optimally active around pH 6 against enamel protein. It is completely inhibited by phenylmethylsulfonyl fluoride and diisopropyl phosphofluoridate, and partially by benzamidine. EDTA does not affect its activity. The enzyme seems to sever initially enamel protein into two segments, one containing lysine, arginine and tyrosine and the other being free from these amino acids.
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