Endogenous Lectins of Bovine Pancreas

Abstract

Affinity chromatography of salt and detergent extracts from bovine pancreas on glycosylated or glycoprotein-linked Sepharose 4B resulted in purification of different carbohydrate-binding proteins. Three species of proteins with molecular masses of 16 kDa [kilodalton], 35 kDa and 64 kDa exhibiting specificity for .beta.-galatosides, but none with preferential specificity for .alpha.-galactosides, were isolated from salt and detergent extracts. No .**GRAPHIC**. was required for binding. Mannan-binding proteins of 37 kDa, 47 kDa and 94 kDa without .**GRAPHIC**. were only found in the salt extract. No other mannan-binding activity could be detected. Fucose-binding proteins of 34 kDa, 62 kDa and 70 kDa exhibiting .**GRAPHIC**. for binding were present in the salt extract and 2 proteins with 62 kDa and 70 kDa in detergent extract. The different fractions showed agglutination activity when assayed with rabbit erythrocytes. Thus, they can be defined as lectins.