Abstract
The pure alpha 1 acid glycoprotein (AGP) preparation from streptozotocin diabetic rat sera showed diminished sialic acid content and lower ratios of galactose to mannose and galactose to fucose. In vivo incorporation of 14C-leucine and 3H-galactose into AGP of control and diabetic animals was studied 30, 60 and 120 min after administration of the radioisotopic precursors. The changed 14C/3H ratio in AGP of diabetic rats suggested disturbed glycosylation of AGP in this disease. Similar activity of UDP-galactose 4-epimerase in control and diabetic rat liver was found suggesting that this enzyme has no influence on the decreased level of serum protein bound galactose.
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