Carbonic anhydrase from Apis mellifera: purification and inhibition by pesticides

Soydan E., Guler A., Bıyık S., ŞENTÜRK M., Supuran C. T., EKİNCİ D.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.32, sa.1, ss.47-50, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 1
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1080/14756366.2016.1232255
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.47-50
  • Anahtar Kelimeler: Apis mellifera, carbonic anhydrase, inhibitor, pesticide, ISOFORMS I, ISOZYMES I, DERIVATIVES, VI
  • Ondokuz Mayıs Üniversitesi Adresli: Evet

Özet

Carbonic anhydrase (CA) enzymes have been shown to play an important role in ion transport and in pH regulation in several organisms. Despite this information and the wealth of knowledge regarding the significance of CA enzymes, few studies have been reported about bee CA enzymes and the hazardous effects of chemicals. Using Apis mellifera as a model, this study aimed to determine the risk of pesticides on Apis mellifera Carbonic anhydrase enzyme (Am CA). CA was initially purified from Apis mellifera spermatheca for the first time in the literature. The enzyme was purified with an overall purification of similar to 35-fold with a molecular weight of similar to 32 kDa. The enzyme was then exposed to pesticides, including tebuconazole, propoxur, carbaryl, carbofuran, simazine and atrazine. The six pesticides dose-dependently inhibited in vitro AmCA activity at low micromolar concentrations. IC50 values for the pesticides were 0.0030, 0.0321, 0.0031, 0.0087, 0.0273 and 0.0165 mu M, respectively. The AmCA inhibition mechanism of these compounds is unknown at this moment.