Purification and characterization of trehalose-hydrolyzing enzymes from thoracic musculature of the american cockroach,Periplaneta americana |
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| Affiliation: | 1. IP Consulting International, Yakima, WA, USA;2. Agriculture Health and Environment Department, Natural Resources Institute, University of Greenwich, Chatham Maritime, Kent ME4 4TB, UK;3. U.S. Department of Agriculture, Agricultural Research Service, 21 Dunbar Rd., Byron, GA 31008, USA;4. University of Montpellier 2, UMR 5236 Centre d’Etudes des agents Pathogènes et Biotechnologies pour la Santé (CPBS), UM1-UM2-CNRS, 1919 Route de Mendes, Montpellier, France;5. Vineland Research and Innovation Centre, 4890 Victoria Avenue North, Box 4000, Vineland Station, Ontario L0R 2E0, Canada;1. Department of Biotechnology, Human Nutrition and Science of Food Commodities, University of Life Sciences in Lublin, Poland;2. Institute of Agrophysics, Polish Academy of Sciences, Department of Natural Environment Biogeochemistry, Doświadczalna 4, 20-290 Lublin, Poland;1. Ministry of Agriculture Key Lab of Molecular Biology of Crop Pathogens and Insects, Zhejiang University, Hangzhou 310058, P.R.China;2. State Key Lab of Rice Biology, Zhejiang University, Hangzhou 310058, P.R.China;3. Institute of Insect Sciences, Zhejiang University, Hangzhou 310058, P.R.China |
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| Abstract: | Trehalose-hydrolyzing enzymes from particulate and cytosolic components of the thoracic musculature of Periplaneta americana were isolated and purified to homogeneity. The molecular weights of the respective enzymes were determined by SDS-polyacrylamide gel electrophoresis and Sephadex G-150 column chromatography and estimated to be 80,000 Da for the cytosolic enzyme whereas the solubilized enzyme of particulate origin has a molecular weight of approx. 110,000 Da. The cytosolic enzyme hydrolyzes a number of α-glycosides in addition to trehalose and, therefore, may be classified as a general α-glucosidase whereas the particulate enzyme exhibits stringent specificity for trehalose. Chemical modification of the particulate trehalase has revealed involvement of carboxyl and imidazole functions in the catalytic mechanism. Of various compounds tested, castanospermine was the most potent inhibitor of the enzyme. |
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