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Clinical Chemistry 45: 47-53, 1999;
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(Clinical Chemistry. 1999;45:47-53.)
© 1999 American Association for Clinical Chemistry, Inc.

Article

Thermal Instability of the Trimeric Structure of the N-terminal Propeptide of Human Procollagen Type I in Relation to Assay Technology

Jette Brandt1, Thomas N. Krogh2, Charlotte H. Jensen1, Jette K. Frederiksen1 and Børge Teisner1,a

Departments of
1 Medical Microbiology and
2 Molecular Biology, University of Odense, Winsløwparken 19, DK-5000 Odense C, Denmark.
a Author for correspondence. Fax 45 65 915267; e-mail b.teisner{at}imbmed.ou.dk.

The N-terminal propeptide of procollagen type I (PINP) appeared in two peaks after size chromatography. The high-molecular weight form was transformed to the low-molecular weight form during incubation at 37 °C, whereas the low-molecular weight form remained unchanged. The PINP concentrations in amniotic fluid and sera remained unchanged during 37 °C incubation when measured using an ELISA; however, concentrations decreased by 89–93% when measured using an RIA. The ELISA:RIA ratio varied from 1.1 to 2.9 in these fluids because of different size distributions and the inability of the RIA to measure the low-molecular weight form. Thermal transition of the high-molecular weight form caused a change in its elution volume but did not change its migration in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Mass spectrometry revealed identical results for both forms. We reached the following conclusions: (a) the trimeric structure of PINP is unstable at 37 °C; (b) the two molecular forms represent intact {alpha}1 chains in trimeric and monomeric forms; (c) thermal transition is an ongoing in vivo process; and (d) this is important in the choice of assay technology.




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