Literature DB >> 19283216

Separation and Characterization of Heterodera glycines Acetylcholinesterase Molecular Forms.

S Chang, C H Opperman.   

Abstract

The composition and biochemical properties of acetylcholinesterases isolated from Heterodera glycines were determined. Heterodera glycines contains three separable AChE molecular forms that can be grouped into two classes corresponding to classes A and C found in some other nematode species. The apparent lack of class B AChE is unusual and may have significant behavioral ramifications. The class C enzyme isolated from H. glycines is similar to that from Meloidogyne arenaria and M. incognita but is somewhat more sensitive to AChE inhibitors such as eserine. Heterodera glycines possesses a larger percentage of its total acetylcholinesterase as class C than other nematodes thus far examined.

Entities:  

Keywords:  Heterodera glycines; acetylcholinesterase; carbamate; enzyme; nematicide; nematode; organophosphate; soybean cyst nematode

Year:  1992        PMID: 19283216      PMCID: PMC2619247     

Source DB:  PubMed          Journal:  J Nematol        ISSN: 0022-300X            Impact factor:   1.402


  3 in total

1.  Joint action of combinations of pollutants on the acetylcholinesterase activity of several marine species.

Authors:  G Bocquené; C Bellanger; Y Cadiou; F Galgani
Journal:  Ecotoxicology       Date:  1995-08       Impact factor: 2.823

2.  A soluble acetylcholinesterase provides chemical defense against xenobiotics in the pinewood nematode.

Authors:  Jae Soon Kang; Dae-Weon Lee; Young Ho Koh; Si Hyeock Lee
Journal:  PLoS One       Date:  2011-04-27       Impact factor: 3.240

3.  Acetylcholinesterase secreted by Anisakis simplex larvae (Nematoda: Anisakidae) parasitizing herring, Clupea harengus: an inverse relationship of enzyme activity in the host-parasite system.

Authors:  Magdalena Podolska; Katarzyna Nadolna
Journal:  Parasitol Res       Date:  2014-04-05       Impact factor: 2.289

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.