CM-cellulose and Agarose chromatography of denatured rat skin collagen show it to contain α1-chains in two distinct molecular weight classes: (α1)l, 1 × 105 daltons; (α1)h, 1.1 × 105 daltons. Pulse labeling in vivo with 3H-proline (G) for short periods, 90 and 120 minutes, shows the (α1)h-chains of acid soluble collage to have nearly double the specific activity of the (α1)l-chains, indicating a precursor-product relationship. However, unlabeled (α1)h has been isolated from the skins by successive extractions, indicating that conversion of (α1)h to (α1)l is neither immediate nor, possibly, complete. Since (α1)h is smaller than the pro-α1 chains of nascent procollagen, it is clear that procollagen is not cleaved in vivo in a single step to collagen. Heightened aggregation properties of the intermediate collagens containing (α1)h suggest that they may have a particular role in fibrillogenesis.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Sep 26 1972|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology