Purification and Characterization of Two -Amylases from Toxoplasma gondii

Authors: Ferrer A.¹; Hoebeke J.²; Bout D.¹

Source: Experimental Parasitology, Volume 92, Number 1, May 1999 , pp. 64-72(9)

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Abstract:

Ferrer, A., Hoebeke, J., and Bout, D. 1999. Purification and characterization of two -Amylases from Toxoplasma gondii.Experimental Parasitology 92, 64–72. Two distinct -amylases have been identified in Toxoplasma gondii. They were purified close to homogeneity from cytoplasmic and membrane fractions. The apparent molecular weight of the cytoplasmic amylase was 22,300 Da and that of the membrane enzyme was 39,600 Da by gel filtration, and 25,000 and 41,000 Da by SDS gel electrophoresis, respectively. The physicochemical and catalytic properties of both enzymes showed them to be very different. Cytoplasmic -amylase had an acid isoelectric point and its optimum pH was pH 5.0; its activity was unaffected by NaCl, Ca²⁺, or EDTA. The membrane -amylase had an isoelectric point of 7.7 and an optimum pH of 8.0. It was affected by Ca²⁺, inhibited by EDTA, and activated eight-fold by NaCl. Both amylases were inactivated by temperatures above 65°C, but cytoplasmic amylase was more resistant to thermal denaturation. Copyright 1999 Academic Press.

Language: English

Document Type: Research article

Affiliations: 1: CJF-INSERM 93–09, Equipe associèe INRA d'Immunologie Parasitaire, UFR des Sciences Pharmaceutiques, 31 Avenue Monge, Tours, 37200, France 2: Laboratoire de Parasitologie, Mycologie et Mèdecine Tropicale, Facultè de Mèdecine, 2 bis Boulevard Tonnellè, Tours cedex, 37032, France

Publication date: 1999-05-01