Clinical Chemistry
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Clinical Chemistry 40: 734-739, 1994;
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Clinical Chemistry, Vol 40, 734-739, Copyright © 1994 by American Association for Clinical Chemistry

Two-site immunoassay of recombinant hirudin based on two monoclonal antibodies

B Mille, O Condamines, JM Herbert, M Maftouh, C Picard, D Dussossoy and B Pau
Immunoanalyse et Innovation en Biologie Clinique, CNRS-UMR 9921, Faculte de Pharmacie, Montpellier, France.

Two monoclonal antibodies (mAbs), 10-2 and 10-5, both directed against recombinant hirudin variant 2-Lys47 (rHV2), were selected for their high affinity and epitopic specificities to develop a two-site immunoassay of rHV2. The mAb concentrations, incubation time, and temperature were optimized. The immunoassay has a detection limit for rHV2 of 45 ng/L in plasma and 30 ng/L in urine. The reactivity of the mAbs was tested against rHV2 and several forms of this protein truncated in the carboxyl terminus. The capture mAb 10-2 was found to be mainly directed against rHV2, whereas tracer mAb 10-5 was independent of the carboxyl-terminal region of the protein. This explains the high specificity of the immunoassay for the 65-amino acid form of hirudin.


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Copyright © 1994 by the American Association for Clinical Chemistry.