Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
1990-2-14
pubmed:abstractText
The concomitant binding of calcium and inorganic phosphate ions by the highly phosphorylated rat dentin phosphophoryn (HP) was measured in the pH range of 7.4-8.5 using an ultrafiltration procedure. HP binds almost exclusively the triply charged PO4(3-)ion, and for each PO4(3-)ion bound, the protein binds about 1.5 additional Ca2+ ions. The protein-mineral ion complex can be described as a protein with two different ligands, Ca2+ ions and calcium phosphate clusters having a stoichiometry of about Ca1.5PO4. The stoichiometry of the bound clusters is similar to amorphous calcium phosphate, indicating that the protein does not sequester crystal embryos of octacalcium phosphate or hydroxyapatite. The protein-mineral ion complex is amorphous by electron diffraction analysis and does not catalyze the formation of a crystalline phase when aged in contact with its solution.
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
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-10; discussion 211
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Binding of calcium and phosphate ions to dentin phosphophoryn.
pubmed:affiliation
University of Texas Health Science Center, Dental Science Institute, Houston 77225.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.