Purification and partial characterization of the type II procollagen synthesized by embryonic cartilage cells.
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Matrix-free cells were prepared from sternal cartilages of 17-day-old chick embryos, and procollagen synthesized and secreted by the cells was isolated by ion exchange chromatography on carboxymethyl cellulose and by gel filtration. The isolated protein was homogeneous by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and it appeared to consist of identical pro- chains linked by interchain disulfide bonds. Amino acid analysis and cyanogen bromide peptide mapping of the purified procollagen demonstrated that it had structures similar to Type II collagen. The amino acid composition was also consistent with the conclusion that the peptide extensions on the pro- chains of procollagen contained amino acid sequences not found in the collagen portion of the molecule. Segment-long-spacing aggregates were prepared from the procollagen, and aggregates demonstrated the same banding pattern as is found in segment-long-spacing aggregates prepared from Type II collagen. The segment-long-spacing aggregates from procollagen revealed, however, the presence of NH2-terminal extensions of about 150 in length. In addition, the procollagen molecules contained irregularly shaped, large extension peptides at the COOH-terminal end of the molecule. 1977.
