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Characterisation of galactosyltransferase isoforms by ion-exchange and lectin affinity chromatography
1Division of Clinical Cell Biology, MRC Clinical Research Centre, Harrow, Middlesex, UK.
Clinica Chimica Acta; International Journal of Clinical Chemistry
|December 30, 1988
Abstract:
Galactosyltransferase (GT) was isolated from human malignant ascitic fluid, and the ion-exchange and lectin affinity chromatographic behaviour of the two isoforms, GTI and GTII, investigated. The effect of neuraminidase on the binding to DEAE-Sephacel and various lectins suggests that GTII, the so-called cancer-specific isoform, is a more sialylated form of GTI.