Characterization of the precursor forms of the 1 and 2 chains of collagen from matrix-free tendon cells. Academic Article

abstract

• 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.

authors

• Prockop, Darwin

published proceedings

• Biochim Biophys Acta

author list (cited authors)

• Uitto, J., Jimenez, S. A., Dehm, P., & Prockop, D. J.

citation count

• 25

complete list of authors

• Uitto, J||Jimenez, SA||Dehm, P||Prockop, DJ

publication date

• August 1972

publisher

• Elsevier  Publisher

published in

• Biochimica et Biophysica Acta: international journal of biochemistry and biophysics  Journal

keywords

• Amino Acids
• Animals
• Carbon Isotopes
• Chick Embryo
• Collagen
• Cysteine
• Cystine
• Electrophoresis, Polyacrylamide Gel
• Hydroxyproline
• Proline
• Sodium Dodecyl Sulfate
• Tendons
• Tritium

PubMed Central ID

• 4672181

Digital Object Identifier (DOI)

• 10.1016/0005-2795(72)90123-7

start page

• 198

end page

• 205

volume

• 278

issue

• 1

URL

• http://dx.doi.org/10.1016/0005-2795(72)90123-7