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1 September 2000 Purification and Specificity of Two α-Glucosidase Isoforms of the Parasitic Protist Trichomonas vaginalis
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Abstract

Two isoforms of α-glucosidase were purified from the parasitic protist Trichomonas vaginalis. Both consisted of 103 kDa subunits, but differed in pH optimum and substrate specificity. Isoform 1 had a pH optimum around 4.5 and negligible activity on glucose oligomers other than maltose, while isoform 2 with a pH optimum of 5.5 hydrolyzed also such substrates at considerable rates. Neither had activity on glycogen or starch. Isoform 1 had a specific activity for hydrolysis of maltose of 30 U/mg protein and isoform 2 101 U/mg protein. The Km values were 0.4 mM and 2.0 mM, respectively. Isoform 2 probably corresponds to the activity detected on the cell surface.

Benno H. Ter Kuile, Ivan Hrdý, Lidya B. Sánchez, and Miklós Müller "Purification and Specificity of Two α-Glucosidase Isoforms of the Parasitic Protist Trichomonas vaginalis," The Journal of Eukaryotic Microbiology 47(5), 440-442, (1 September 2000). https://doi.org/10.1111/j.1550-7408.2000.tb00072.x
Received: 2 September 1999; Accepted: 15 April 2000; Published: 1 September 2000
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