Purification and characterization of acetylcholinesterase isozymes from the latex of Synadenium grantii Hook, 'f'

Govindappa, T. and Govardhan, L. and Jyothy, P.S. and Veerabhadrappa, P.S. (1987) Purification and characterization of acetylcholinesterase isozymes from the latex of Synadenium grantii Hook, 'f'. Indian Journal of Biochemistry & Biophysics, 24 (4). pp. 209-317. ISSN 0301-1208

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Abstract

Three acetylcholinesterase isoenzymes were purified from S. grantii latex by a combination of acetone fractionation, CM-​Sephadex C-​50 chromatog., Sephadex G-​200 gel filtration, and PE-​Cellulose chromatog. The homogeneity of the isoenzymes was established by PAGE and isoelectrofocusing. The pI values were 5.0, 5.2, and 5.4. The mol. wt. of each enzyme was estd. to be 70,​000 by a gel-​filtration method. SDS-​PAGE indicated that each enzyme consisted of 2 subunits of mol. wt. ∼35,​000. These enzymes were glycoproteins and were more sensitive towards carbamate inhibitors compared to organophosphates. They exhibited substrate inhibition and showed identical substrate specificity and inhibitor sensitivity. The rate consts. for different inhibitors were calcd. These 3 enzymes were considered to be charge isoenzymic forms of the latex acetylcholinesterase.

Item Type: Article
Subjects: Faculty of Science > Environmental and Biological Sciences > Biochemistry
Divisions: Jnana Bharathi / Central College Campus > Department of Biochemistry
Depositing User: Mr . Chandrashekar
Date Deposited: 14 Sep 2016 09:10
Last Modified: 14 Sep 2016 09:10
URI: http://eprints-bangaloreuniversity.in/id/eprint/5629

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