Linked Life Data

9084653

Source:http://linkedlifedata.com/resource/pubmed/id/9084653

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
1997-5-15
pubmed:abstractText
This study was undertaken to examine probable initial pathway(s) of amelogenin proteolysis, making comparisons between species and thus searching for a common theme. Specimens of developing dental enamel matrix were obtained from (i) mouse, 6 days post natal, (ii) male pig, (iii) female bovine, (iv) rat, and (v) female human. In collaboration with the Mass Spectrometry Facility of the School of Pharmacy, University of California, San Francisco, samples of the lyophilized proteins were analyzed by liquid chromatography-mass spectrometry. The results were complex, a large number (15-30 components) being identified in each case. Mass values obtained for each sample were compared with computed values derived from segments of the known amino acid sequences for the principal amelogenins of the five species. Putative identity with an experimental figure was accepted when the mass numbers agreed to within +/-2.0 daltons. In each case it was found that some components could be identified with sequences of the parent amelogenin. In the case of the mouse and rat strong evidence was obtained for sequential proteolytic processing from the carboxy-terminus of both the 180 and 156 residue amelogenins. A comparison between the five species showed, a fragment (cow, man, pig and mouse) uniquely identified as being derived by the processing of the parent amelogenin to the first proline residue from the carboxy-terminus, leading to the cleavage of 11 residues of the anionic carboxy-terminal sequence. In addition, it was found in each case, that mass identity of experimental data with the known sequences was only obtained assuming the presence of a single phosphorylated residue.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Comparative mass spectrometric analyses of enamel matrix proteins from five species suggest a common pathway of post-secretory proteolytic processing.
pubmed:affiliation
Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, Los Angeles 90033, USA. alanfinc@zygote.hsc.usc.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.