Characterization of the precursor forms of the 1 and 2 chains of collagen from matrix-free tendon cells.
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The precursor form of collagen known as "procollagen" or "transport form" was recovered from the incubation medium of matrix-free cells from embryonic tendon. The polypeptide chains of the collagen were separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and examined by amino acid analysis. The results indicated that the additional peptides on both the pro-1 and pro-2 chain contained about 130 residues of amino acids and were similar in composition. Labeling of the polypeptide chains with [14C] cystine indicated that the pro-1 and the pro-2 chains contained about the same amount of cystein or cystine. 1972.
author list (cited authors)
Uitto, J., Jimenez, S. A., Dehm, P., & Prockop, D. J.
complete list of authors
Uitto, J||Jimenez, SA||Dehm, P||Prockop, DJ