| Literature DB >> 283119 |
Abstract
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 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.Entities:
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Year: 1979 PMID: 283119 DOI: 10.1177/00220345790580023001
Source DB: PubMed Journal: J Dent Res ISSN: 0022-0345 Impact factor: 6.116