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Haemolymph proteins and lipoproteins in lepidoptera—A comparative electrophoretic study

1974; Elsevier BV; Volume: 47; Issue: 1 Linguagem: Inglês

10.1016/0305-0491(74)90092-3

0305-0491

Elaine Whitmore, Lawrence I. Gilbert,

Insect Pest Control Strategies

1. Polyacrylamide gel electrophoresis of haemolymph from seven species of Lepidoptera (Hyalophora cecropia, H. gloveri, Callosamia promethea, Philosamia cynthia, Antheraea polyphemus, A. mylitta, Manduca sexta) reflected the close relationship between species within the same genus and the differences between the saturniids and a sphingid. 2. Comparisons were made of ontogenetic protein pattern changes in the larval-pupal-adult development of P. cynthia (a saturniid) and M. sexta (a sphingid). 3. With the exception of M. sexta, it was possible to recognize the sex of pupae and adults from the electropherograms by the presence of a major protein in the haemolymph of pupal and adult females which is absent from or present in lower concentration in the males. In all seven species, the total protein concentration of the haemolymph is higher in females than in males. 4. All species examined have haemolymph lipoproteins, and all the haemolymph lipoproteins of H. cecropia, H. gloveri, P. cynthia, C. promethea and A. polyphemus are also glycoproteins. Several proteins and lipoproteins possessing esterase activity were detected in the larval or pupal haemolymph of M. sexta, H. gloveri, H. cecropia, P. cynthia and A. mylitta.