The enamel proteins prepared from porcine enamel samples at an early stage of development are separated at least 4 fractions by Sephadex G-100 gel filtration at pH 10.8. The main components of secondary and fourthly-eluted fraction were further purified by ion exchange chromatography. The results of sequence analyses of these proteins by sequential Edman degradation and by hydrolysis with carboxypeptidase Y showed that the partial amino acid sequences of these proteins were iden tical.
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