Biosynthesis of a low molecular weight collagen by rabbit growth plate cartilage organ cultures

Analysis of [14C]-proline labeled proteins synthesized by organ cultures of rabbit growth plate cartilage slices revealed that this tissue synthesized a low molecular weight collagen in addition to Type II, 1 alpha, 2 alpha, and 3 alpha collagens. This collagen appears to be a distinct molecular species on the basis of electrophoretic mobility, hydroxyproline content and cyanogen bromide peptide mapping. In subsequent studies, a non-disulfide-bonded, higher molecular weight form of the same molecule was identified.