Procollagen assembly and secretion in embryonic chick bone.

Chick embryo skull bones incorporated radioactive proline and cystein into procollagen in short term organ culture. Pulse-chase experiments showed that individual precursor chains (pro-alpha1 and pro-alpha2) were formed first and that these were subsequently linked by disulfide bounds into trimers. Radioautography showed that labeled material was secreted 30 min after adding label to the cells, and electrophoretic analyses showed that after this time completed labeled collagen molecules appeared. Conversion from disulfide-linked procollagen to collagen proceeded in more than one step. An intermediate form consisting of shorter chains, which were still trimerically linked, was found.