Comparison of the recombinant glucosephosphate isomerase from different zymodemes of Entamoeba histolytica with their natural counterparts by isoenzyme electrophoresis

E. Razmjou, M. Rezaian, A. Haghighi, B. Kazemi, B. Farzami, S. Kobayashi, T. Nozaki

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Entamoeba histolytica is the etiological agent of invasive amoebiasis, the third leading parasitic cause of mortality in the world. Our aim was to find a molecular correlation between a glucosephosphate isomerase zymodeme analyses in E. histolytica zymodemes. It was demonstrated that natural and recombinant glucosephosphate isomerase enzymes of E. histolytica comigrated in the starch gel electrophoresis, indicating that the isoenzyme pattern of E. histolytica glucosephosphate isomerase could be explained from the primary sequences alone and means that expression of the polypeptides of the described sequences in Escherichia coli are able to reproduce the classical glucosephosphate isomerase isoenzyme patterns.

Original languageEnglish
Pages (from-to)35-40
Number of pages6
JournalIranian Journal of Public Health
Volume34
Issue number4
Publication statusPublished - 2005

Fingerprint

Glucose-6-Phosphate Isomerase
Entamoeba histolytica
Isoenzymes
Electrophoresis
Starch Gel Electrophoresis
Amebiasis
Escherichia coli
Peptides
Mortality
Enzymes

Keywords

  • Entamoeba histolytica
  • Glucosephosphate isomerase
  • Zymodemes

ASJC Scopus subject areas

  • Public Health, Environmental and Occupational Health

Cite this

Comparison of the recombinant glucosephosphate isomerase from different zymodemes of Entamoeba histolytica with their natural counterparts by isoenzyme electrophoresis. / Razmjou, E.; Rezaian, M.; Haghighi, A.; Kazemi, B.; Farzami, B.; Kobayashi, S.; Nozaki, T.

In: Iranian Journal of Public Health, Vol. 34, No. 4, 2005, p. 35-40.

Research output: Contribution to journalArticle

Razmjou, E. ; Rezaian, M. ; Haghighi, A. ; Kazemi, B. ; Farzami, B. ; Kobayashi, S. ; Nozaki, T. / Comparison of the recombinant glucosephosphate isomerase from different zymodemes of Entamoeba histolytica with their natural counterparts by isoenzyme electrophoresis. In: Iranian Journal of Public Health. 2005 ; Vol. 34, No. 4. pp. 35-40.
@article{0e062c024898471baa3801c744408c17,
title = "Comparison of the recombinant glucosephosphate isomerase from different zymodemes of Entamoeba histolytica with their natural counterparts by isoenzyme electrophoresis",
abstract = "Entamoeba histolytica is the etiological agent of invasive amoebiasis, the third leading parasitic cause of mortality in the world. Our aim was to find a molecular correlation between a glucosephosphate isomerase zymodeme analyses in E. histolytica zymodemes. It was demonstrated that natural and recombinant glucosephosphate isomerase enzymes of E. histolytica comigrated in the starch gel electrophoresis, indicating that the isoenzyme pattern of E. histolytica glucosephosphate isomerase could be explained from the primary sequences alone and means that expression of the polypeptides of the described sequences in Escherichia coli are able to reproduce the classical glucosephosphate isomerase isoenzyme patterns.",
keywords = "Entamoeba histolytica, Glucosephosphate isomerase, Zymodemes",
author = "E. Razmjou and M. Rezaian and A. Haghighi and B. Kazemi and B. Farzami and S. Kobayashi and T. Nozaki",
year = "2005",
language = "English",
volume = "34",
pages = "35--40",
journal = "Iranian Journal of Public Health",
issn = "0304-4556",
publisher = "Iranian Journal of Public Health",
number = "4",

}

TY - JOUR

T1 - Comparison of the recombinant glucosephosphate isomerase from different zymodemes of Entamoeba histolytica with their natural counterparts by isoenzyme electrophoresis

AU - Razmjou, E.

AU - Rezaian, M.

AU - Haghighi, A.

AU - Kazemi, B.

AU - Farzami, B.

AU - Kobayashi, S.

AU - Nozaki, T.

PY - 2005

Y1 - 2005

N2 - Entamoeba histolytica is the etiological agent of invasive amoebiasis, the third leading parasitic cause of mortality in the world. Our aim was to find a molecular correlation between a glucosephosphate isomerase zymodeme analyses in E. histolytica zymodemes. It was demonstrated that natural and recombinant glucosephosphate isomerase enzymes of E. histolytica comigrated in the starch gel electrophoresis, indicating that the isoenzyme pattern of E. histolytica glucosephosphate isomerase could be explained from the primary sequences alone and means that expression of the polypeptides of the described sequences in Escherichia coli are able to reproduce the classical glucosephosphate isomerase isoenzyme patterns.

AB - Entamoeba histolytica is the etiological agent of invasive amoebiasis, the third leading parasitic cause of mortality in the world. Our aim was to find a molecular correlation between a glucosephosphate isomerase zymodeme analyses in E. histolytica zymodemes. It was demonstrated that natural and recombinant glucosephosphate isomerase enzymes of E. histolytica comigrated in the starch gel electrophoresis, indicating that the isoenzyme pattern of E. histolytica glucosephosphate isomerase could be explained from the primary sequences alone and means that expression of the polypeptides of the described sequences in Escherichia coli are able to reproduce the classical glucosephosphate isomerase isoenzyme patterns.

KW - Entamoeba histolytica

KW - Glucosephosphate isomerase

KW - Zymodemes

UR - http://www.scopus.com/inward/record.url?scp=31744431588&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=31744431588&partnerID=8YFLogxK

M3 - Article

VL - 34

SP - 35

EP - 40

JO - Iranian Journal of Public Health

JF - Iranian Journal of Public Health

SN - 0304-4556

IS - 4

ER -