Abstract
Direct comparison of type X collagen synthesized by human sheep and chick growth-plate cartilage has shown that the human type X collagen is similar to the chick in both its molecular mass, containing component α-chains of 59 kDa with helical regions of 45 kDa and apparent absence of disulphide-stabilized aggregates, whereas the sheep type X collagen has slightly larger α-chains (63 kDa) accounted for by a longer helical region (49 kDa) that contains cystine residues essential for the formation of the high-mo]ecular-mass aggregates found with this species. Type X collagen from all three species showed heterogeneity in primary collagen structure as revealed by Staphylococcus aureus V8 proteinase-generated peptide maps. Collagen synthesis by growth-plate cartilage in culture particularly synthesis of type IX and X collagen was shown to be very sensitive to prior storage and suggests caution in thc interpretation of changes detected when examining collagen synthesis by growth plates in culture.
Original language | English |
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Pages (from-to) | 513-520 |
Number of pages | 8 |
Journal | Biochemical Journal |
Volume | 277 |
Issue number | 2 |
DOIs | |
Publication status | Published or Issued - 1991 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology