Porcine amelogenins

Abstract

Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.

DOI: 10.1007/BF00316293

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@article{Yamakoshi1994PorcineA, title={Porcine amelogenins}, author={Yasuo Yamakoshi and Takako Tanabe and Makoto Fukae and Masaharu Shimizu}, journal={Calcified Tissue International}, year={1994}, volume={54}, pages={69-75} }