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New PDF release: Biochemistry of Insects

By Morris Rockstein

ISBN-10: 012591640X

ISBN-13: 9780125916400

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Example text

Migratoria, C. erthyrocephala, and A. mellifera. The hormone has been partially characterized and shown to be a polypeptide secreted by the corpora cardiaca. It is believed to be synthe­ sized in the intrinsic neurosecretory cells of the corpora cardiaca or in the cerebral neurosecretory cells. The hormone appears to act through cyclic AMP to activate glycogen phosphorylase (Section VIII, B, 1). Table IV illustrates the effect of cardiacectomy and allatectomy on the hemolymph trehalose concentration of adults of C.

Table III shows that trehalase is widely distributed between larval, pupal, and adult tissues. This enzyme has been found to exist in two distinct forms in insect tissues: free in the cytosol (soluble trehalase), and bound to mem­ branes of cell organelles (particulate trehalase). The soluble enzyme is found primarily in the intestine, whereas the particulate one is associated mainly with muscle mitochondria. Although the subcellular locations of the particu­ late trehalase need further study, it is becoming increasingly evident that the mitochondrial membrane is an important location.

The production of mutants of D. melanogaster which are deficient in cytosolic GPDH and incapable of flight has shown the importance of the glycerol 3-phosphate shuttle in flight metabolism. The enzyme has a homodimeric structure being made up of two subunits each with a molecular weight of about 32,000. The cytosolic GPDH of D. melanogaster has been separated into several isoenzymes which, although derived from the same structural gene, are present in different proportions in larval and adult tissues.

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Biochemistry of Insects by Morris Rockstein


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