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    Öğe
    In vitro inhibition of purified human carbonic anhydrase I and II by novel fluorene derivatives
    (Macedonian Journal of Chemistry and Chemical Engineering, 2014) Demirhan, Hulya; Arslan, Mustafa; Kaya, Mustafa Oguzhan; Kaya, Yesim; Gencer, Nahit; Arslan, Oktay
    In this study, 9-benzylidene-9H-fluorene-substituted urea (5a-p) and thiourea derivatives (5q-v) were synthesized and their inhibitory effects on the activity of human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II were purified from human erythrocytes using a Sepharose 4B-L-tyrosine-sulphanilamide affinity column. All the synthesized compounds inhibited the activity of the hCA I and II isoenzymes. Among the synthesized compounds, 5f was found to be the most active (IC50 = 21.4 ?M) for inhibition of hCA I and 5s was the most active (IC50 = 25.3 ?M) for inhibition of hCA II.
  • [ X ]
    Öğe
    IN VITRO INHIBITION OF PURIFIED HUMAN CARBONIC ANHYDRASE I AND II BY NOVEL FLUORENE DERIVATIVES
    (Soc Chemists Technologists Madeconia, 2014) Demirhan, Hulya; Arslan, Mustafa; Kaya, Mustafa Oguzhan; Kaya, Yesim; Gencer, Nahit; Arslan, Oktay
    In this study, 9-benzylidene-9H-fluorene-substituted urea (5a-p) and thiourea derivatives (5q-v) were synthesized and their inhibitory effects on the activity of human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II were purified from human erythrocytes using a Sepharose 4B-L-tyrosine-sulphanilamide affinity column. All the synthesized compounds inhibited the activity of the hCA I and II isoenzymes. Among the synthesized compounds, 5f was found to be the most active (IC50 = 21.4 mu M) for inhibition of hCA I and 5s was the most active (IC50 = 25.3 mu M) for inhibition of hCA II.