Abstract
C-reactive protein (C-RP) was purified from harbor seal (Phoca vitulina) serum by calcium dependant phosphoryl-choline and protein A affinity chromatography. Polyacrylamide gel electrophoresis under reducing conditions revealed a single protein moiety with a molecular weight of approximately 25 kDa. An internal peptide derived from tiffs purified protein was subjected to N-terminal amino acid sequencing. A high amino acid sequence similarity was obtained with other published mammalian C-RP molecules confirming that the purified protein was a C-RP homologue. Eight specific monoclonal antibodies (P13, P51, P87, P101, P106, P130, P157 and P219) were raised against this purified protein. All 8 monoclonal antibodies immunoblotted with the 25 kDa C-RP subunit under reducing conditions. A competitive immunoassay was developed identifying elevated C-RP concentrations in harbor seal serum samples with clinical evidence of inflammatory disease. Application of this immunoassay for the measurement C-RP may provide valuable information for the clinical assessment of harbor seal health.
Original language | English (US) |
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Pages (from-to) | 151-162 |
Number of pages | 12 |
Journal | Veterinary Immunology and Immunopathology |
Volume | 59 |
Issue number | 1-2 |
DOIs | |
State | Published - Oct 6 1997 |
Keywords
- Acute phase
- C-reactive protein
- Harbor seal
- Immunoassay
- Inflammation
- Monoclonal antibody
ASJC Scopus subject areas
- Animal Science and Zoology
- Immunology
- veterinary(all)