title: Characterisation of galactosyltransferase isoforms by ion-exchange and lectin affinity chromatography.
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.
authors.affiliation: Division of Clinical Cell Biology, MRC Clinical Research Centre, Harrow, Middlesex, UK.
authors.forename: F A
authors.initials: FA
authors.lastname: Boyle
authors.forename: T J
authors.initials: TJ
authors.lastname: Peters
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D002852:Chromatography, Ion Exchange; D005700:Galactosyltransferases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D007527:Isoenzymes / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D037102:Lectins; D009439:Neuraminidase / Q000494:pharmacology
chemical_list: D007527:Isoenzymes; D037102:Lectins; D005700:Galactosyltransferases; D009439:Neuraminidase