Abstract
A simple, reproducible gel-filtration procedure for the isolation of one of the major ‘J-Group’ polypeptides of the bovine foetal dental-enamel matrix is described. The purified polypeptide was characterized by amino acid analysis, electrophoresis, cleavage with CNBr and N-terminal analyses. The isolated component is shown to be closely similar to an amelogenin component described by other workers.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
5 articles.
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