High-Performance Liquid Chromatographic Characterization of Two Lichen Lectins with Arginase Activity Differing in Their Glycosyl Moiety

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Abstract
Two isolectins from the lichen Xanthoria parietina, one of them retained by the thallus and another secreted from the thallus to the medium, both showing arginase activity, have been purified to homogeneity. Ethanol-soluble products obtained after acidic hydrolysis of both proteins have been analyzed by HPLC under isocratic conditions using acetonitrile-water (80:20, v/v) as mobile phase. Detection is performed by measurement of UV absorbance at 195 nm, using a highly sensitive detector. Purification of standard sugars by filtering aqueous solutions through an activated alumina column is absolutely required. The glycosyl moiety of secreted arginase is composed by galactose and glucose whereas that of thalline enzyme contains N-acetyl-D-glucosamine and glucose.

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