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Purification and properties of the anionic form of alpha-galactosidase from germinating guar (Cyamopsis tetragonolobus).

Shivanna, B. D. and Ramakrishna, M. and Ramadoss, C. S. (1990) Purification and properties of the anionic form of alpha-galactosidase from germinating guar (Cyamopsis tetragonolobus). Plant Science, 72 (2). 173-180 ; 27 ref..

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Abstract

Three forms of alpha-galactosidase occur in germinating guar representing 100% of the activity present. They are alpha-galactosidase-A (anionic, 28%), alpha-galactosidase-C1 (cationic, 12%) and alpha-galactosidase-C2 (cationic, 60%). The second major form of alpha-galactosidase (the anionic form) from germinating guar was purified to near homogeneity. It has a mol. wt. of 97 000 and consists of 2 identical subunits each of Mr 42 000. The physicochemical, kinetic and immunological properties of this enzyme were studied in comparison with the major cationic alpha-galactosidase present in germinating guar. The molecular size of alpha-galactosidase-A was only half of alpha-galactosidase-C2 as judged by gel filtration studies. Both forms were found to be glycoproteins, but their carbohydrate content and composition were quite different. The analysis of amino acid composition showed a striking dissimilarity with respect to glutamic acid, methionine, histidine and arginine content. There were distinct differences in their kinetic properties as well. The polyclonal antibody raised against alpha-galactosidase-C2 did not show any cross reactivity with alpha-galactosidase-A showing that the 2 forms are immunologically distinct.

Item Type: Article
Uncontrolled Keywords: ENZYMES-; GALACTOSIDASES-; LEGUMES-; VEGETABLES-; alpha-GALACTOSIDASES
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Fermentation Technology and Bioengineering
Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Mar 2011 09:36
Last Modified: 28 Dec 2011 10:01
URI: http://ir.cftri.com/id/eprint/7984

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