Co-Authors:
Neubauer, I., Division of Entomology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Ishaaya, I., Division of Entomology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Aharonson, N., Division of Pesticide Chemistry, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Raccah, B., Division of Virology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Abstract:
1. 1. The optimum conditions for trehalase activity of either soluble or membrane-bound trehalase of both apterous and alate morphs of Aphis citricola were determined. 2. 2. Sodium deoxycholate (DOC) act as a solubilizing agent for membrane-bound trehalase, with no appreciable effect on its activity. 3. 3. Alates exhibit about a 50% higher level of soluble protein compared with that of apterase. Trehalase activity of this fraction in alates is 70-85% higher than that in apterase, as determined per mg protein or per aphid. The activity of the membrane-bound trehalase was on the same level in both morphs when determined relative to mg protein. 4. 4. The relative high activity of the soluble trehalase in alates may reflect an increased energy supply needed for sustaining physical activity involved in aphid flight. © 1980.