Cyclosporin G and metabolite binding to cyclophilin and a 50-kDa binding protein related to in vitro immunosuppression

Autor:	J. G. Donnelly, E. W. Palaszynski, Yajun Chen, R. W. Yatscoff, K. R. Copeland, S. J. Soldin
Rok vydání:	1993
Předmět:	Binding protein Metabolite Biochemistry (medical) Clinical Biochemistry Biological activity Biology In vitro Dissociation constant chemistry.chemical_compound Biochemistry chemistry Cyclosporin a Potency Cyclophilin
Zdroj:	Clinical Chemistry. 39:122-125
ISSN:	1530-8561 0009-9147
Popis:	Seven purified metabolites of cyclosporin G (CsG) were studied for binding to cyclophilin and a 50-kDa binding protein (50-kDa BP). The ratios of the metabolite dissociation constants with respect to CsG were compared with in vitro immunosuppression by using the primary mixed lymphocyte suppression assay. The immunosuppressive potency ratio of the parent compounds, both cyclosporin A (CsA) and CsG, compared favorably with the drug dissociation constants for cyclophilin and the 50-kDa BP. Three of the seven metabolites had comparable binding and potency ratios for the 50-kDa BP. In contrast, none of the seven metabolites appreciably bound to cyclophilin in the concentration range tested.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ccb75b3ba8192910b4028e3ec47803fa https://doi.org/10.1093/clinchem/39.1.122 Zobrazit plný text záznamu