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Endogenous lectins of bovine pancreas


Hoppe-Seyler's Zeitschrift für Physiologische Chemie 365(6): 633-638
Endogenous lectins of bovine pancreas
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.


Accession: 005358086

PMID: 6479893

DOI: 10.1515/bchm2.1984.365.1.633



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