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1.
Indian J Exp Biol ; 2003 Jun; 41(6): 598-602
Article in English | IMSEAR | ID: sea-58920

ABSTRACT

The studies on binding of hexachlorocyclohexane (HCH) with carrier proteins were carried out to establish the role of proteins in the transport of insecticides in insects. Sephadex G-200 column chromatography resolved haemolymph of adult male desert locust, Schistocerca gregaria into three major protein peaks. There was significant binding of gamma-HCH with first protein peak (F1). Two classes of binding sites were observed on first protein peak for gamma-HCH. However low level of binding was observed with the third protein peak (F3) of the haemolymph. Bindings of HCH-isomers (alpha, beta and gamma) with bovine serum albumin (BSA) were not related to their water solubilities. Moderate to low affinities (1.4 -1.84 x 10(6) M(-1)) of HCH-isomers for BSA were observed. The present studies showed that more HCH binds to haemolymph lipoprotein of locust as compared to BSA. This indicates a significant role of haemolymph proteins in the transport of insecticides in insects.


Subject(s)
Animals , Cats , Grasshoppers , Insect Proteins/physiology , Isomerism , Hexachlorocyclohexane/chemistry
2.
Indian J Exp Biol ; 1992 Sep; 30(9): 846-9
Article in English | IMSEAR | ID: sea-57056

ABSTRACT

Binding of alpha-, beta-, gamma-hexachlorocyclohexane, p,p'-DDT and p,p'-DDE with bovine serum albumin (BSA) and locust brain homogenate was studied. Binding affinities of pesticides were higher for the locust brain homogenates than for BSA. Results of uptake by isolated locust brain revealed higher uptake of gamma-HCH than alpha-HCH. gamma-HCH uptake was also higher from locust haemolymph than either from BSA or from buffer.


Subject(s)
Animals , Brain/metabolism , Cattle , Grasshoppers/metabolism , Hydrocarbons, Chlorinated , Insecticides/metabolism , Nerve Tissue Proteins/metabolism , Protein Binding , Serum Albumin, Bovine/metabolism
3.
Indian J Biochem Biophys ; 1992 Jun; 29(3): 299-302
Article in English | IMSEAR | ID: sea-27722

ABSTRACT

A yellow lipoprotein was isolated and purified from haemolymph of desert locust, Schistocerca gregaria Forskal, by precipitation at low ionic concentration and by gel filtration. Sephadex G-200 resolved haemolymph into five protein peaks. First peak was of lipoprotein with molecular weight of 501,000 +/- 7000 (n = 3) and on electrophoresis, it separated into three bands. Maximum lipids from lipoprotein could be extracted with chloroform: methanol solvent system and were 52% by weight.


Subject(s)
Animals , Chromatography, Gel , Desert Climate , Electrophoresis, Disc , Grasshoppers , Hemolymph/chemistry , Lipoproteins/chemistry , Male
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