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 25 kDa amelogenin indicated that porcine 25 kDa amelogenin is neither phosphorylated nor glycosylated.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.