Linked Life Data

3105842

Source:http://linkedlifedata.com/resource/pubmed/id/3105842

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-6-9
pubmed:abstractText
Absence of precipitation of calcium phosphate salts onto tooth surfaces from human saliva, which is supersaturated with respect to calcium phosphate salts, has been attributed in part to the presence in the salivary secretions of a group of acidic proline-rich phosphoproteins (PRP). These macromolecules are considered to act by adsorbing onto dental enamel where they inhibit surface-induced precipitation of calcium phosphate salts. The inhibitory activity is known to be associated primarily with the amino-terminal region of the PRP. The aim of this study was to determine the features of the primary structure of this molecular segment responsible for inhibitory activity. The 30-residue, amino-terminal segment of PRP-3, which contains the two phosphoserines and 11 of the 13 carboxyl groups present in PRP-3, was obtained by tryptic digestion. This peptide, designated PRP-3(TI), was treated with thermolysin to give the monophosphopeptides, Val-PSer-Gln-Glu-Asp-Val-Pro and Leu-Val-Ile-Ser-Asp-Gly-Gly-Asp-PSer-Glu-Gln, and with alkaline phosphatase to give the dephosphorylated analog, PRP-3(TI)DP. The inhibitory activities of PRP-3(TI) and the derived peptides, a synthetic peptide, phosphoseryl-phosphoserine (PSer-PSer), and O-phosphoserine (PSer), were determined using an assay based on inhibition of seeded precipitation of calcium phosphate. Inhibitory activities, expressed as concentrations of inhibitors required to give standard inhibitory activities, were PRP-3(TI), 0.59 microM; PSer-PSer, 3.5 microM; the two monophosphopeptides, 29 and 32.5 microM; PRP-3(TI)DP, 56 microM; PSer, 329 microM.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/PRH1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proline-Rich Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Thermolysin, http://linkedlifedata.com/resource/pubmed/chemical/alpha-tricalcium phosphate, http://linkedlifedata.com/resource/pubmed/chemical/calcium phosphate, http://linkedlifedata.com/resource/pubmed/chemical/dicalcium phosphate anhydrous, http://linkedlifedata.com/resource/pubmed/chemical/monocalcium phosphate, http://linkedlifedata.com/resource/pubmed/chemical/tetracalcium phosphate
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0171-967X
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
126-32
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Inhibition of calcium phosphate precipitation by human salivary acidic proline-rich proteins: structure-activity relationships.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.