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

Zulfiqar A. Malik, Sumaira Amir

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish (US)
Pages (from-to)1779-1788
Number of pages10
JournalApplied Biochemistry and Biotechnology
Volume165
Issue number7-8
DOIs
StatePublished - Dec 1 2011

Fingerprint

Grasshoppers
Hemolymph
Proteins
Lipoproteins
Molar mass
Sodium dodecyl sulfate
Chromatography
Polyacrylates
Electrophoresis
Lipids
Ion exchange
Gels
Molecular weight
Locusta migratoria
Membranes
Ion Exchange
Reverse-Phase Chromatography
Cellular Immunity
Sodium Dodecyl Sulfate
Insects

Keywords

  • Apolipophorin III
  • Hemolymph
  • Locusta migratoria
  • Schistocerca gregaria

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

Cite this

An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria. / Malik, Zulfiqar A.; Amir, Sumaira.

In: Applied Biochemistry and Biotechnology, Vol. 165, No. 7-8, 01.12.2011, p. 1779-1788.

Research output: Contribution to journalArticle

Malik, Zulfiqar A. ; Amir, Sumaira. / An apolipophorin III protein from the hemolymph of desert locust, Schistocerca gregaria. In: Applied Biochemistry and Biotechnology. 2011 ; Vol. 165, No. 7-8. pp. 1779-1788.
@article{aff8b49c494c47beb690cd0339585b7c,
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",
year = "2011",
month = "12",
day = "1",
doi = "10.1007/s12010-011-9394-9",
language = "English (US)",
volume = "165",
pages = "1779--1788",
journal = "Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology",
issn = "0273-2289",
publisher = "Humana Press",
number = "7-8",

}

TY - JOUR

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.

KW - Apolipophorin III

KW - Hemolymph

KW - Locusta migratoria

KW - Schistocerca gregaria

UR - http://www.scopus.com/inward/record.url?scp=81955167908&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=81955167908&partnerID=8YFLogxK

U2 - 10.1007/s12010-011-9394-9

DO - 10.1007/s12010-011-9394-9

M3 - Article

C2 - 21976149

AN - SCOPUS:81955167908

VL - 165

SP - 1779

EP - 1788

JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

JF - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

SN - 0273-2289

IS - 7-8

ER -