Abstract
1.1. The higher molecular weight, (HMW, Mr 140 kDa) acid phosphatase (AcPase) of the frog liver (Rana esculenta) was separated into enzymatically active components by isoelectric focusing in an immobilized pH gradient and their carbohydrate chains were analyzed by specific lectin binding after native blotting.2.2. The lectin-binding patterns obtained with ConA, WGA, LcH and PNA as well as with WGA and PNA after desialylation indicate that the frog liver HMW AcPase contains predominantly N-linked complex and/or hybride type carbohydrate chains with terminal sialic acid and fucose residues; O-glycosylated enzyme components with free and sialic acid substituted Gal-GalNAc sequences were also detected.
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