gamma-Glutamyltransferase is eliminated from the circulation via the asialoglycoprotein receptor in liver. After purifying the enzyme from human liver, a subfractionation into differently sialylated forms was obtained using MonoQ ion exchange chromatography. The uptake of such forms from rat circulation was studied and the slowest rate was measured for the most sialylated form. To test if the uptake of the sialylated enzymes was dependent on prior desialylation in the circulation the enzyme was recovered from liver after uptake and from serum after inhibiting the uptake with asialofetuin. Analysis of these recovered forms showed no apparent alteration in charge. The enzyme is apparently eliminated without prior desialylation through available galactose units which bind with low affinity to the receptor.