An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria

Zulfiqar A. Malik; Sumaira Amir

doi:10.1007/s12010-011-9394-9

An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria

Zulfiqar A. Malik, Sumaira Amir

Biochemistry and Molecular Medicine

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

Apolipophorin III (apoLp-III) from insects and apolipoprotein A-I from humans, are major component of the lipoprotein and share various properties. ApoLp-III is an abundant hemolymph protein. Besides its crucial role in lipid transport, apoLp-III is able to associate with fungal and bacterial membranes and stimulate cellular immune responses. ApoLp-III was isolated and purified from the hemolymph of desert locust Schistocerca gregaria by ion-exchange and reversed-phase chromatography. The purity and the molecular weight of apoLp-III were determined at ∼19,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. According to similarities in the amino terminal sequence, molar mass and retention on reversed-phase analytical HPLC column, this protein is a Schistocerca gregaria homologue of Locusta migratoria apoLp-III.

Original language	English (US)
Pages (from-to)	1779-1788
Number of pages	10
Journal	Applied Biochemistry and Biotechnology
Volume	165
Issue number	7-8
DOIs	https://doi.org/10.1007/s12010-011-9394-9
State	Published - Dec 1 2011

Keywords

Apolipophorin III
Hemolymph
Locusta migratoria
Schistocerca gregaria

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology

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title = "An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria",

abstract = "Apolipophorin III (apoLp-III) from insects and apolipoprotein A-I from humans, are major component of the lipoprotein and share various properties. ApoLp-III is an abundant hemolymph protein. Besides its crucial role in lipid transport, apoLp-III is able to associate with fungal and bacterial membranes and stimulate cellular immune responses. ApoLp-III was isolated and purified from the hemolymph of desert locust Schistocerca gregaria by ion-exchange and reversed-phase chromatography. The purity and the molecular weight of apoLp-III were determined at ∼19,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. According to similarities in the amino terminal sequence, molar mass and retention on reversed-phase analytical HPLC column, this protein is a Schistocerca gregaria homologue of Locusta migratoria apoLp-III.",

keywords = "Apolipophorin III, Hemolymph, Locusta migratoria, Schistocerca gregaria",

author = "Malik, {Zulfiqar A.} and Sumaira Amir",

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T1 - An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria

AU - Malik, Zulfiqar A.

AU - Amir, Sumaira

PY - 2011/12/1

Y1 - 2011/12/1

N2 - Apolipophorin III (apoLp-III) from insects and apolipoprotein A-I from humans, are major component of the lipoprotein and share various properties. ApoLp-III is an abundant hemolymph protein. Besides its crucial role in lipid transport, apoLp-III is able to associate with fungal and bacterial membranes and stimulate cellular immune responses. ApoLp-III was isolated and purified from the hemolymph of desert locust Schistocerca gregaria by ion-exchange and reversed-phase chromatography. The purity and the molecular weight of apoLp-III were determined at ∼19,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. According to similarities in the amino terminal sequence, molar mass and retention on reversed-phase analytical HPLC column, this protein is a Schistocerca gregaria homologue of Locusta migratoria apoLp-III.

AB - Apolipophorin III (apoLp-III) from insects and apolipoprotein A-I from humans, are major component of the lipoprotein and share various properties. ApoLp-III is an abundant hemolymph protein. Besides its crucial role in lipid transport, apoLp-III is able to associate with fungal and bacterial membranes and stimulate cellular immune responses. ApoLp-III was isolated and purified from the hemolymph of desert locust Schistocerca gregaria by ion-exchange and reversed-phase chromatography. The purity and the molecular weight of apoLp-III were determined at ∼19,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. According to similarities in the amino terminal sequence, molar mass and retention on reversed-phase analytical HPLC column, this protein is a Schistocerca gregaria homologue of Locusta migratoria apoLp-III.

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KW - Schistocerca gregaria

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