Document Detail


Isolation and chemical characterization of the phosphoproteins of chicken bone matrix: heterogeneity in molecular weight and composition.
MedLine Citation:
PMID:  3801434     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ethylenediaminetetraacetic acid and HCl extracts of calcified chicken bone were fractionated by a variety of techniques, including molecular sieving in guanidinium chloride, ion-exchange chromatography on DEAE-cellulose, high-performance liquid chromatography (HPLC), reverse-phase HPLC, and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using several different experimental schemas, we isolated 14 apparently homogeneous components varying in molecular weight from approximately 150K to approximately 4K-5K. The compositions of all of the phosphoproteins were characterized by high concentrations of Asp, Glu, Ser, Gly, and Ala. Seven of the components which were analyzed contained concentrations of carbohydrate varying from approximately 4% to approximately 17%. Three of the components containing O-phosphoserine which behaved as single bands on SDS-PAGE with molecular weights of approximately 150K, approximately 90K, and approximately 70K contained Hyp and Hyl or Hyl alone and may represent covalently bonded or strongly associated collagen-phosphoprotein complexes or hydroxylated Pro and/or Lys residues of the phosphoproteins. The findings that the amino acid compositions of several of the components were very similar and that N-terminal partial amino acid sequences of the approximately 90- and approximately 60-kilodalton (kDa) and of the approximately 150- and approximately 32-kDa components, respectively, were identical make it clear that some of the lower molecular weight components are derived by proteolysis from higher molecular weight species. In addition to proteolysis, we speculate that it is possible, from the N-terminal amino acid sequence data and preliminary cross-reaction studies of antibodies to four of the phosphoproteins, that the heterogeneity observed in the phosphoprotein components may also be due in part to there being more than one independent gene product for chicken bone phosphoproteins.
Authors:
A Uchiyama; M Suzuki; B Lefteriou; M Glimcher
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  25     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1986 Nov 
Date Detail:
Created Date:  1987-03-16     Completed Date:  1987-03-16     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7572-83     Citation Subset:  IM; S    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Bone Matrix / analysis*
Chickens
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Molecular Weight
Phosphoproteins / isolation & purification*
Grant Support
ID/Acronym/Agency:
34078//PHS HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Phosphoproteins

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


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