Shoeb Ahmad

Antitermite Activities of C. decidua Extracts and Pure Compounds against Indian White Termite Odontotermes obesus (Isoptera: Odontotermitidae)

In the present investigation, we have tested antitermite responses of Capparis decidua stem, root, flower, and fruit extracts and pure compounds to Odontotermes obesus in various bioassays. Crude stem extract has shown very high susceptibility and very low LD50 values, that is, 14.171 μg/mg in worker termites. From stem extract, three pure compounds were isolated in pure form namely, heneicosylhexadecanoate (CDS2), triacontanol (CDS3), and 2-carboxy-1, 1-dimethylpyrrolidine (CDS8) which have shown very low LD50 value in a range of 5.537–10.083 μg/mg. Similarly, one novel compound 6-(1-hydroxy-non-3-enyl)-tetrahydropyran-2-one (CDF1) was isolated from flower extract that has shown an LD50 8.08 μg/gm. Repellent action of compounds was tested in a Y-shaped glass olfactometer in which CDF1 compounds have significantly repelled termites to the opposite arm. Besides this, C. decidua extracts have shown significant reduction ( and 0.01) in termite infestation in garden saplings when it was coated on cotton tags and employed over tree trunks. Further, C. deciduas stem extract was used for wood seasoning, which gave very good results as test wood sticks have shown significantly ( and 0.01) very low termite infestation.

Production of polyclonal antibodies against Indian honeybee (Apis indica) venom toxins and its efficacy in reversal of toxic effects

In this study, the efficiency of polyclonal anti-honeybee venom (HBV) antibody was successfully explored in the form of reversal of toxic effects induced by the venom. Honeybee venom expresses its toxicity not only by allergic reactions but it also causes molecular toxicity by making alteration in enzymes and bio-molecules. To come out from these toxic effects, polyclonal antibodies were generated by immunizing albino mice. Antibody was partially purified by octanoic acid precipitation and by ammonium sulphate treatment. The presence of antibody in the antiserum was confirmed by immuno-double diffusion test. 40% of LD50 of bee venom was incubated with 400, 800, and 1200 µg of purified antibody and this incubated mixture was injected into experimental mice. Parallel to this, one set of mice were injected with only 40% of LD50 and another injected with only saline which was considered as the control. The venom injected group showed 89.69% decrease in serum protein content while free amino acid, uric acid, cholesterol, pyruvic acid, total lipid and glucose was increased by 112.5, 122.10,102.48,110.0, 125.0 and 107.22% respectively. Subsequently, venom dose also elevated serum ACP, ALP, GPT, GOT, LDH up to 126.92, 128.44, 136.66, 109.09, and 114.24%. Contrarily, it depleted the AchE activity. On the other hand, the group of experimental animals that received 40% of LD50 of venom incubated with purified antiserum showed a complete reversal of the above abnormalities in the content of serum bio-molecules and enzymes.

Immuno-histochemical localization of cholesterol binding proteins in Schistocerca gregaria (Forskal)

This manuscript aims to investigate immunocytochemical localization of cholesterol binding proteins (CBPs) in semi-thin sections of midgut of Schistocerca gregaria (Forskal). For this purpose, polyclonal antibody specific to CBPs were raised in albino mice and used in immuno-fluorescence and immuno-blotting to determine the cellular location of CBPs. Midgut tissue sections were incubated with pAbs anti-cholesterol binding protein (primary antibody) and finally associate them with HRP conjugated anti-rabbit immunoglobulin (secondary antibody). Semi thin tissue sections of midgut portion were stained with hematoxylin and eosin for establishing general morphology of epithelial cells in control sections. Positive control tissue sections were stained with Sudan Black-B for microscopic visualization of cholesterol binding sites. Further, cholesterol association in tissue sections was confirmed by using tetramethylrhodamine isothiocyanate (TRITC) labeled florescent antibodies and immuno-blotting of CBPs. Finally, CBPs or cholesterol-carrying proteins were detected intracellularly in midgut epithelial/ microvillus cells named as CBP+. Zymogene like dense granules localized were found scattered throughout the apical portion of microvillus cells. Further, presence of these CBPS was confirmed by SDS-PAGE gel electrophoresis and immuno-blotting. In treatments, dietary cholesterol was found to be internalized bound to complexed with CBPs before absorption. Further, same protein was also localized in other tissues like fat body, testis, and ovary of male and female insects of S. gregaria. However, present study done on immuno-cytochemical localization of cholesterol binding proteins in microvillus cells confirms that CBPS are main careers of cholesterol. These proteins also assist in transport of cholesterol to the various organs after its subsequent absorption. Keywords: Cholesterol binding proteins (CBPs), cholesterol, lipoprotein, midgut, immunocytochemical localization, S. gregaria (Forskal). African Journal of Biotechnology Vol 13(28) 2884-2896