Studies on the agglutinating activity of pancreatic extracts and its relevance to function

Agglutination of washed rabbit erythrocytes caused by pancreatic acinar cell extract was inhibited by glucose, maltose and cellobiose. Process of elimination and purification divulged that the acinar cell enzyme alpha-amylase was responsible for attributing the agglutinin activity. Assay of enzyme and agglutinin activity data of different fractions of re-purified alpha-amylase eluted from HPLC column showed that both the activity resides in the same fraction which suggests that the enzyme binds to the glucosyl residues of the rabbit erythrocytes via the carbohydrate binding/catalytic sites. Similar properties of other glycosidases were also noted.