Abstract
In order to gain information on the ability of Schizosaccharomyces pombe to process heterologous glycoproteins, the heterologous invertase, obtained from the expression in Schiz. pombe of the SUC2 gene of Saccharomyces cerevisiae, was characterized. In Schiz. pombe the heterologous invertase is secreted into the cell wall and seems to be firmly bound to this structure. After the isolation of the heterologous invertase the study of its enzymatic characteristics revealed that it is more similar to the Sacch. cerevisiae external invertase than to the Schiz. pombe invertase. However, it is glycosylated like the Schiz. pombe invertase since it reacts with the lectin from Bandeiraea simplicifolia seeds conjugated to fluorescein isothiocyanate, which indicates the presence of terminal galactose residues in the enzyme. Moreover, the presence of galactose in the heterologous invertase has been confirmed after analysis of the sugars present in its carbohydrate moiety by gas liquid chromatography.
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