Development of an assay for the quantification of type I collagen synthesis in the guinea pig

Helen L. Quasnichka*, John F. Tarlton, Janet M. Anderson-MacKenzie, M. E J Billingham, Allen J. Bailey, Andrew R. Pickford

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


There is a need for a reliable assay for the quantification of collagen type I synthesis in the guinea pig, an important model for many connective tissue diseases. Procollagen type I C-terminal propeptide (PICP) is the established marker of type I collagen synthesis but, to date, no assay has been developed to measure PICP in guinea pig tissue extracts. A monoclonal antibody, known to cross-react with intact guinea pig procollagen type I (anti-PICP), was tested for its ability to bind soluble guinea pig PICP in crude skin extracts using a biosensor. Anti-PICP was immobilised to the surface of a sensor chip and antibody-antigen binding was detected using the phenomenon of surface plasmon resonance (SPR). The binding component in the SPR-immunoassay was identified as PICP by purification and N-terminal sequencing. Guinea pig PICP was purified from skin by gel filtration, ion exchange chromatography and lectin affinity chromatography. Purified PICP was then biotinylated and used with anti-PICP to develop a competition ELISA that was able to selectively and sensitively measure PICP in extracts of guinea pig connective tissue.

Original languageEnglish
Pages (from-to)133-141
Number of pages9
JournalJournal of Immunological Methods
Issue number1-2
Publication statusPublished - Feb 2005


  • Collagen type I synthesis
  • Competition ELISA
  • Guinea pig
  • PICP
  • SPR


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