Document Detail


In vivo decomposition of phosphoserine and serine in noncollagenous protein from human dentin.
MedLine Citation:
PMID:  3926273     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
HCl-soluble proteins in human dentin ranging in age from 3 to 45 years exhibit amino acid compositional changes consistent with beta-elimination and hydrolysis of phosphoserine as well as dehydration and aldol cleavage of serine. This is the first evidence of nonenzymatic mechanisms for in vivo degradation of hydroxy and substituted hydroxy amino acids in dentin. Decomposition of phosphoseryl residues reduces the calcium-binding capacity of phosphoproteins. Elimination and dehydration reactions can produce variability in molecular weight. The rates of decomposition may be rapid enough to cause the heterogeneity or "maturational" degradation seen in dentin phosphoproteins during mineralization.
Authors:
P M Masters
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Calcified tissue international     Volume:  37     ISSN:  0171-967X     ISO Abbreviation:  Calcif. Tissue Int.     Publication Date:  1985 May 
Date Detail:
Created Date:  1985-09-16     Completed Date:  1985-09-16     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7905481     Medline TA:  Calcif Tissue Int     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  236-41     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adolescent
Adult
Age Factors
Aspartic Acid / metabolism
Child, Preschool
Dentin / metabolism*
Humans
Isoelectric Point
Kinetics
Phosphoproteins / metabolism*
Serine / metabolism
Stereoisomerism
Grant Support
ID/Acronym/Agency:
DE06896/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Phosphoproteins; 56-45-1/Serine; 56-84-8/Aspartic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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