The effects of some bromophenols on human carbonic anhydrase isoenzymes

TASLIMI P., GÜLÇİN İ., OZTASKIN N., ÇETİNKAYA Y., GÖKSU S., Alwasel S. H., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.4, ss.603-607, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 4
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1054820
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.603-607
  • Anahtar Kelimeler: Bromophenols, carbonic anhydrase, enzyme inhibition, enzyme purification, isoenzymes, IN-VITRO ANTIOXIDANT, TROUT ONCORHYNCHUS-MYKISS, INHIBITORY PROPERTIES, SULFONAMIDE DERIVATIVES, LIPID-PEROXIDATION, CAFFEIC ACID, ISOZYMES I, ISOFORMS I, PURIFICATION, MELATONIN
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrases (CAs, EC 4.2.1.1), which are involved in a variety of physiological and pathological processes, are ubiquitous metalloenzymes mainly catalyzing the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3-) and proton (H+). In this study, a dozen of bromophenol derivatives (1-12) were evaluated as metalloenzyme CA (EC 4.2.1.1) inhibitors against the human carbonic anhydrase isoenzymes I and II (hCA I and II). Cytosolic hCA I and II isoenzymes were effectively inhibited by bromophenol derivatives (1-12) with K-is in the low nanomolar range of 1.85 +/- 0.58 to 5.04 +/- 1.46 nM against hCA I and in the range of 2.01 +/- 0.52 to 2.94 +/- 1.31 nM against hCA II, respectively.