Abstract
Polyacrylamide gel electrophoresis of galactosyltransferase (GT) extracted from a human colon adenocarcinoma cell line, HCT-8, demonstrated the presence of two peaks of activity: a slow-moving peak, referred to as GT-II, and a more anodally migrating peak, designated as GT-I, which was also found for normal human serum. However, if GT solubilized from HCT-8 cells was separated by isoelectric focusing, no unique isoenzymes could be detected. Total GT activity from HCT-8 cells was purified by α-lactalbumin-Sepharose affinity chromatography followed by ion exchange chromatography on either DEAE-cellulose or FPLC using a Mono Q anion exchange resin. Three major peaks of activity were resolved from anion exchange chromatography. Electrophoresis of each peak revealed a GT pattern identical with that originally observed for the crude (detergent) solubilized homogenate. No enrichment of either GT-I or GT-II was observed in the three enzyme fractions. The data suggest that GT-II may be an artifactual activity of cancer cells composed of GT-I associated with some contaminating protein.
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