Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 33: 32-37, 1987;
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Quesniaux, V.
Right arrow Articles by van Regenmortel, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Quesniaux, V.
Right arrow Articles by van Regenmortel, M. H.

Clinical Chemistry, Vol 33, 32-37, Copyright © 1987 by American Association for Clinical Chemistry

Potential of monoclonal antibodies to improve therapeutic monitoring of cyclosporine

V Quesniaux, R Tees, MH Schreier, G Maurer and MH van Regenmortel

We show that monitoring of cyclosporine by immunoassay could be improved by using monoclonal antibodies (MAbs) of restricted specificity instead of polyclonal antisera that recognize both unmodified cyclosporine and its metabolites. MAbs with high affinity for cyclosporine have been prepared and characterized. We tested their ability to discriminate between native cyclosporine and its metabolites in indirect solid-phase enzyme immunoassay with a set of cyclosporine metabolites modified at residues 1, 4, 6, and 9 (corresponding to the six known sites of metabolism of cyclosporine). All the metabolites tested were detected by MAb1 at least 15- to 1000-fold less well than unmodified cyclosporine. A second MAb recognized unmodified cyclosporine and most of its metabolites equally well. Both MAbs retained their activity when coupled to alkaline phosphatase and could therefore be used in a direct solid-phase enzyme immunoassay.


The following articles in journals at HighWire Press have cited this article:


Home page
 J. Biol. Chem.Home page
M. Demeule, R. M. Wenger, and R. Beliveau
Molecular Interactions of Cyclosporin A with P-glycoprotein. PHOTOLABELING WITH CYCLOSPORIN DERIVATIVES
J. Biol. Chem., March 7, 1997; 272(10): 6647 - 6652.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1987 by the American Association for Clinical Chemistry.