Partial amino acid sequences of two proteins in developing porcine enamel.
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 identical.
D000566:Amelogenesis; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D003743:Dental Enamel / Q000032:analysis; D003746:Dental Enamel Proteins / Q000032:analysis*; D013552:Swine
D000596:Amino Acids; D003746:Dental Enamel Proteins