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Evidence for a Terminal -d-Galactopyranosyl Residue in Galactosylgalactosylglucosylceramide from Human Kidney

From the ¹ From the Donner Laboratory of Experimental Neurochemistry, Montreal Neurological Institute, Montreal 112, Canada
² From the Department of Chemistry, McGill University, Montreal 110, Canada

Galactosylgalactosylglucosylceramide (CTH) was extracted and purified from pooled normal human kidney tissue and also from the kidney of a patient with Fabry's disease, a glycosphingolipid storage disease characterized by a defect in the catabolism of CTH. Nuclear magnetic resonance spectra of the intact molecules were recorded at 100 and 220 MHz in pyridine-d₅ at various temperatures. The characteristics of signals attributable to the anomeric protons are consistent with the following structural features: a ß-d-glucopyranosyl residue linked to ceramide (H-1, doublet, = 4.74 ppm, J = 7.6 Hz);an internal, ß-d-galactopyranosyl residue (H-1, doublet, = 4.94 ppm, J = 7.5 Hz);a terminal -d-galactopyranosyl residue (H-1, doublet, = 5.45 ppm, J = 4.1 Hz). Optical rotatory data are also consistent with such a formulation for the glycolipid. CTH and lactosylceramide labeled in the terminal d-galactosyl moiety were prepared by oxidation with the enzyme d-galactose oxidase (EC 1.1.3.-) and reduction of the resulting hexodialdoses with [³H]NaBH₄. With the use of these substrates, it was found that the terminal d-galactosidic linkage of CTH, but not of lactosylceramide, was hydrolyzed by partially purified -d-galactoside galactohydrolase (EC 3.2.1.22) from green coffee beans. These physicochemical and enzymic data are presented as proof that the terminal d-galactopyranosyl residue of the CTH of human renal tissue has the stereoconfiguration.

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