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  • Title: Purification and specificity of two alpha-glucosidase isoforms of the parasitic protist Trichomonas vaginalis.
    Author: Ter Kuile BH, Hrdý I, Sánchez LB, Müller M.
    Journal: J Eukaryot Microbiol; 2000; 47(5):440-2. PubMed ID: 11001140.
    Abstract:
    Two isoforms of alpha-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.
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