Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1977-5-20
pubmed:abstractText
Calcium-binding and biochemical studies have been applied to characterize the state of the carboxylate and protein-bound phosphate groups in the EDTA-demineralized matrices of rat bone and dentine. The organic phosphate and carboxylate content of demineralized bone is virtually identical to that of purified steer skin collagen whereas demineralized dentine has a significantly higher phosphate and carboxylate content, presumably due to the presence of an acidic non-collagenous phosphoprotein. Two classes of calcium-binding sites can be detected in demineralized bone, demineralized dentine, and purified, reconstituted collagen. The number of strong calcium-binding sites correlates with the number of protein-bound phosphate groups. Depending on the preparative procedure, seven to nine such sites (per collagen molecule) are present in dentine, and one to two in the purified reconstituted collagen and in bone. The binding constant for the dentinal sites (1.1 X 10(4) M-1), however, is 20 times greater than that for bone or reconstituted collagen fibrils from skin. We tentatively conclude that the strong calcium-binding site in bone and reconstituted collagen is of the form protein-PO-4Ca++ whereas in dentine it is of the form protein (formula: see text); the weak binding sites in bone and dentine are of the form protein-COO-Ca++; and that approximately 160 of the 217 carboxylate groups of the collagen molecules of dentine or bone are present as electrostatic linkages of the form protein-COO-+H3N-protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0008-0594
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
275-84
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
On the state of anionic groups of demineralized matrices of bone and dentine.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.