Advanced Search

Journal Navigation

Journal Home

Subscriptions

Archive

Contact Us

Table of Contents

CiteULike is a free service for managing and discovering scholarly references - click here to get started.

Sign In to gain access to subscriptions and/or personal tools.
Journal of Dental Research
This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to Saved Citations
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Request Reprints
Right arrow Add to My Marked Citations
Citing Articles
Right arrow Citing Articles via Google Scholar
Right arrow Citing Articles via Scopus
Google Scholar
Right arrow Articles by Butler, W.T.
Right arrow Articles by Richardson, W.S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Butler, W.T.
Right arrow Articles by Richardson, W.S.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*(L)-ASPARTIC ACID
*L-SERINE
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Dentin Proteins: Chemistry, Structure and Biosynthesis

W.T. Butler

University of Alabama in Birmingham, Birmingham, Alabama 35294, U.S.A.

E.C. Munksgaard

University of Alabama in Birmingham, Birmingham, Alabama 35294, U.S.A.

W.S. Richardson

University of Alabama in Birmingham, Birmingham, Alabama 35294, U.S.A.

One of the most abundant noncollagenous proteins of dentin is a phosphoprotein rich in aspartic acid and phosphoserine. This protein occurs in soluble and inextractable forms, the latter being associated with the insoluble collagenous matrix. This protein is capable of tightly binding a relatively high level of calcium. Biosynthetic and radioautographic data suggest that shortly after its biosynthesis, the phosphoprotein is transported and bound to the collagen at the predentin-dentin junction. This event is probably central to the mineralization process, though other glycoproteins may be involved.

Journal of Dental Research, Vol. 58, No. 2 suppl, 817-824 (1979)
DOI: 10.1177/00220345790580023301
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?