Porcine amelogenins.
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 25 kDa amelogenin indicated that porcine 25 kDa amelogenin is neither phosphorylated nor glycosylated.
Yamakoshi
Y
Y
Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.
Tanabe
T
T
Fukae
M
M
Shimizu
M
M
D053523:Amelogenin; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D003746:Dental Enamel Proteins / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013552:Swine; D014083:Tooth Germ; D014158:Transcription, Genetic
D053523:Amelogenin; D003746:Dental Enamel Proteins; D003546:Cysteine Endopeptidases; C019913:clostripain; D003488:Cyanogen Bromide