Tülin ARSLAN, Köksal KÜÇÜKAKYÜZ, Bekir ÇÖL, Göçmen Belgin TAŞKIN, Vatan TALKIN

The biochemical basis of insecticide resistance and determination of esterase enzyme patterns by using page in field collected populations of Drosophila melanogaster from Muğla province of Turkey

Biyokimyasal ve moleküler biyoloji teknikleri, doğal populasyonlarda, potansiyel veya gelişmekte olan direnç mekanizmaları hakkında çok spesifik bilgiler sağlamaktadır. Bu araştırmada, Muğla ve ilçelerinden toplanan Drosophila melanogaster populasyonlarında glutatyon-S-transferaz (GST), yüzde kalan asetilkolin esteraz (AChE) ve genel esteraz aktiviteleri ölçülmüştür. Bununla birlikte poliakrilamid jel elektroforezi (PAGE) yöntemi kullanılarak örneklerdeki esteraz enzim profilleri belirlenmiştir. Yüzde kalan asetilkolin esteraz enzim aktivitesi incelenen örneklerde duyarlı soya göre yüksek bulunmuştur, a ve (3-naftil asetatın substrat olarak kullanılması ile toplam 21 esteraz bandı elde edilmiştir, bu bantların 18 tanesi a esteraz, iki tanesi (3 esteraz ve bir tanesi ise a/B esteraz olarak sınıflandırılmıştır.

Muğla ve ilçelerine ait Drosophila melanogaster populasyonlarında insektisit direncinin biyokimyasal temellerinin ve esteraz enzim profilinin PAGE yšntemi kullanılarak belirlenmesi

Biochemical and molecular biology methods provide more specific information about the resistance potential or the development of resistance in field populations of living organisms. In this research, the enzymatic activities of Glutathione-S-transferase (GST), percent remaining acetylcholinesterase (AChE) and general esterase were measured in Drosophila melanogaster populations collected from different towns of Muğla Province. Furthermore, esterase enzyme patterns of these populations were determined by using polyacrylamide gel electrophoresis (PAGE). Percent remaining activities of AChE were found to be significantly higher in all strains compared to the activities of the susceptible one. Twenty one different esterase bands were detected when a- and (3-naphtyl acetate were used as substrates and the bands were classified as 18 a-esterases, 2 (3-esterases and 1 a/(3 esterase.

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