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Validation of an automated intact N-terminal propeptide of type I procollagen (PINP) assay |
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| Authors: | Koivula Marja-Kaisa Richardson Jill Leino Aila Valleala Heikki Griffiths Katie Barnes Alex Konttinen Yrjö T Garrity Martha Risteli Juha |
| Affiliation: | aInstitute of Diagnostics, Department of Clinical Chemistry, P.O. Box 5000, 90014 University of Oulu, Finland and Central Hospital of Kainuu Region, Kajaani, Finland;bImmunodiagnostic Systems Ltd (IDS Ltd), 10 Didcot Way, Business Park Boldon, Tyne & Wear NE35 9PD, UK;cTYKSLAB, Hospital District of Southwest Finland and Department of Clinical Chemistry, Turku University Central Hospital, Kiinamyllynkatu 4-8, 20520 Turku, Finland;dDepartment of Medicine, Helsinki University Central Hospital, 00029 Helsinki, Finland;eORTON Orthopaedic Hospital of the ORTON Foundation, Helsinki, Finland;fCOXA Hospital for Joint Replacement, Tampere, Finland;gInstitute of Diagnostics, Department of Clinical Chemistry, P.O. Box 5000, 90014 University of Oulu, Finland |
| Abstract: | ObjectivesN-terminal propeptide of type I procollagen assay (PINP) reflects the rate of type I collagen synthesisDesign and methodsDifferent sera were fractioned by gel filtration and analyzed with intact and total PINP assays. The sizes of the antigens were determined by western blotting. The thermal stability was tested at + 37 °C, + 4 °C and room temperature (RT).ResultsAutomated intact PINP assay hardly measured monomeric form. In haemodialysis patients intact and total PINP assays gave significantly different results. The monomeric PINP antigen in serum was larger than the trimeric PINP antigen. PINP were thermally stable at least 7 days at + 4 °C and at RT but the results of both assays were decreased similarly at + 37 °C.ConclusionsThe IDS-iSYS intact PINP assay is precise and sensitive. It seems that monomeric form is not derived from the thermal instability of the trimers but acts as a confounding factor. |
| Keywords: | Type I collagen Propeptide Automated assay Total PINP Intact PINP |
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