Abstract
Bone and dentin collagen are less susceptible to solubilization by pepsin digestion than is skin collagen. Digestion at 4°C for 72 h solubilized only 35.3% of bovine cortical bone and 5.6% of bovine dentin compared with nearly 100% dissolution of bovine skin. Sodium dodecyl sulfate-acrylamide gel electrophoresis and molecular sieve chromatography showed that, for bone and dentin, intact α chains and cross-linked aggregates of β, γ and higher weight remained intact after pepsin solubilization but lower molecular weight fragments also were prevalent indicating chain scission in helical regions. Electron microscopic examination of segment long spacing precipitates of the soluble collagens confirmed the presence of solubilized polymerized collagen. The principal reducible cross-link in both bone and dentin was the precursor of dihydroxylysinonorleucine and this cross-link was also present in the solubilized collagens. Small amounts of non-collagenous proteins and glycosaminoglycans of different compositions in dentin and bone resisted extraction before pepsin digestion. However, the differences in solubilization of the collagens have been related to differences in cross-linkage placement.
Original language | English (US) |
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Pages (from-to) | 177-192 |
Number of pages | 16 |
Journal | BBA - Protein Structure |
Volume | 491 |
Issue number | 1 |
DOIs | |
State | Published - Mar 28 1977 |
Externally published | Yes |
Funding
This work was supportedb y grants from the Medical ResearchC ouncil of Canada (to D. J. C.) and Grant DE-01374 from the National Institute of Dental ResearchU, .S.A. (to A. V.).
ASJC Scopus subject areas
- General Medicine