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Studies on electrophoretic protein patterns of fat body, haemolymph and ovary in an indian fresh water-bug, Laccotrephes rubra Linn. (Nepidae: Heteroptera)

Published online by Cambridge University Press:  19 September 2011

P. R. Yadav  and
Dinesh Kumar
P. R. Yadav
Affiliation:
Department of Zoology, Banaras Hindu University, Varanasi-221 005, India
Dinesh Kumar
Affiliation:
Department of Zoology, Banaras Hindu University, Varanasi-221 005, India
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Abstract

Polyacrylamide disc gel electrophoresis (PAGE) was performed on soluble proteins from the fat body, haemolymph (male and female), and ovary of the adult fresh water-bug, Laccotrephes rubra, in order to determine their protein patterns. The electrophoresis resulted in the separation of 16 and 17 protein components in male and female haemolymph respectively. In female fat body extracts 15 protein bands could be detected; whereas ovary extracts resolved into 11 protein bands only. Comparison of the electropherograms of protein pattern of fat body (FBPP), haemolymph (HPP) and ovary (OPP) revealed that the extra band present in the female haemolymph is common to both female fat body and ovary, which is suggestive of it being the female specific protein, i.e. vitellogenin. A careful examination of the various electropherograms further revealed that the majority of the protein bands of haemolymph and ovary are common to its corresponding fat body protein bands. This might suggest that the ovary derives most of its protein components from the surrounding haemolymph, which have presumably been synthesized and secreted by the fat body.

The histochemical analyses demonstrated that the female-specific protein band is a glycolipoprotein; and most of the haemolymph protein zones stain as glycoprotein, lipoprotein or ribonucleoprotein. ‘Stains-all’ technique however, revealed the presence of four possible RNA bands in fat body extracts.

Résumé

On procéda à une électrophorèse par gel polyacrylamide en disque (PAGE) sur des protéines solubles provenant de corps gras, de l'hémolymphe (mâle et femelle) et de l'ovaire de la punaise d'eau couce adulte, Laccotrephes rubra, afin de déterminer les modèles de protéines. L'électrophorèse permit d'identifier 16 et 17 composants protéiques dans l'hémolymphe mâle et femelle respectivement. Les extraits de corps gras femelles montraient 15 bandes protéiques, ceux de l'ovaire n'en montrant que 11. la comparaison des electrophorégrammes des modéles de protéines des corps gras (FBPP), de l'hémolymphe (HPP) et de l'ovaire (OPP) fait apparaître que la bande supplémentaire présente dans l'hémolymphe femelle se retrouve également dans les corps gras femelles et dans l'ovaire, ce qui permet de supposer qu'elle est la protéine spécifique femelle, c'est-à-dire la vitellogenèse. Un examen attentif des divers electrophorégrammes révéla par ailleurs que la majorité des bandes protéiques de l'hémolymphe et de l'ovaire se retrouvent dans ceux des corps gras leur correspondant. Ceci pourrait indiquer que l'ovaire obtient la plupart de ses composants protéiques de l'hémolymphe qui l'entoure, composants synthétisés et sécrétés par les corps gras.

Les analyses histochimiques démontrent que la protéine femelle spécifique est une glycolipoprotéine; et que la plupart des bandes protéiques de l'hémolymphe sont des glycoprotéines, des lipoprotéines ou des ribonucléoprotéines. Cependant la technique au stainsall révèle la présence de 4 bandes RNA possibles dans les extraits de corps gras.

Keywords

Electrophoretic patternsfat bodyhaemolymphovaryModèles par électrophorèsecorps grashémolympheovaire
Type
Research Articles
Information
International Journal of Tropical Insect Science , Volume 7 , Issue 5 , October 1986 , pp. 599 - 604
Copyright
Copyright © ICIPE 1986

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