Abstract
Type X Collagen was extracted with 1 M NaCl and 10 mM dithiothreitol at neutral pH from fetal human growth plate cartilage and purified to homogeneity by gel filtration and anion‐exchange chromatography. The purified protein migrates in SDS/polyacrylamide gels with an apparent Mr of 66000 under reducing conditions, and as a high‐Mr oligomer under non‐reducing conditions. Purified collagenase digests most of the molecule; pepsin digestion at 4°C decreases the Mr of the monomer to 53000. A rabbit antiserum was raised against purified human type X collagen; the IgG fraction was specific for this collagen by criteria of ELISA and immunoblotting after absorption with collagen types I, II, VI, IX and XI. Immunohistological studies localized type X collagen exclusively in the zone of hypertrophic and calcifying cartilage.
Original language | English (US) |
---|---|
Pages (from-to) | 575-580 |
Number of pages | 6 |
Journal | European Journal of Biochemistry |
Volume | 196 |
Issue number | 3 |
DOIs | |
State | Published - Mar 1991 |
ASJC Scopus subject areas
- Biochemistry