Comparison of alfa-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet
2010
Dojnov, B., Institute of Chemistry, Tehnology and Metallurgy, Belgrade (Serbia) | Lončar, N., Faculty of Chemistry, Belgrade (Serbia) | Božić, N., Institute of Chemistry, Tehnology and Metallurgy, Belgrade (Serbia) | Nenadović, V., Institute for Biological Research Sinisa Stankovic, Belgrade (Serbia) | Ivanović, J., Institute for Biological Research Sinisa Stankovic, Belgrade (Serbia) | Vujčić, Z., Faculty of Chemistry, Belgrade (Serbia)
Alfa-amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI less than 3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa.
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