Clinical Chemistry
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Clinical Chemistry 40: 811-816, 1994;
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Clinical Chemistry, Vol 40, 811-816, Copyright © 1994 by American Association for Clinical Chemistry

Purification of human procollagen type I carboxyl-terminal propeptide cleaved as in vivo from procollagen and used to calibrate a radioimmunoassay of the propeptide

BJ Pedersen and M Bonde
Center for Clinical & Basic Research, Ballerup, Denmark.

We purified human procollagen type I carboxyl-terminal propeptide (PICP) that had been cleaved as in vivo from procollagen. PICP in serum- free medium from cultured human fetal fibroblasts was purified by thiophilic adsorption chromatography, low-pressure gel filtration, and HPLC gel filtration. The purity and homogeneity of the protein was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino-terminal amino acid sequencing showed that the sequences of the alpha 1 and alpha 2 chains of this PICP were identical to those of the PICP produced in vivo. The monocomponent PICP thus purified was used as calibrator in a simple equilibrium-type RIA of PICP with polyclonal antibodies raised in rabbits. The measuring range is 0.15-3.75 nmol/L, and the assay detection limit is 0.03 nmol/L. The within-run and total CVs are 2% and 4%, respectively. The reference interval for the plasma concentration of PICP in healthy women of ages > 30 years is 0.36-1.44 nmol/L (geometric mean 0.72 nmol/L, n = 154).


The following articles in journals at HighWire Press have cited this article:


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 J. Biol. Chem.Home page
K. Beck, B. A. Boswell, C. C. Ridgway, and H. P. Bachinger
Triple Helix Formation of Procollagen Type I Can Occur at the Rough Endoplasmic Reticulum Membrane
J. Biol. Chem., August 30, 1996; 271(35): 21566 - 21573.
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