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 α-amylase was responsible for attributing the agglutinin activity. Assay of enzyme and agglutinin activity data of different fractions of re-purified α-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.
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Hedeskov CJ: Mechanism of glucose-induced insulin secretion. Physiol Rev 60: 442–509, 1980
Malaisse WJ, Sener A, Malaisse-Lagae F: Insulin release: reconciliation of the receptor and metabolic hypotheses. Molec Cell Biochem 37: 157–165, 1981
Lacy PE, Kostianovsky M: Method for the isolation of intact islets of Langerhans from the rat pancreas. Diabetes 16:35–39,1967
MarChis-Mouren G, Pasero L, Desnuelle P: Further studies on amylase biosynthesis by pancreas of rats fed on a Starch-rich or a casein-rich diet. Biochem Biophys Res Comm 13: 262–266, 1963
Marchis-Mouren G, Pasero L: Isolation of two amylases in porcine pancreas. Biochim Biophys Acta 140: 366–368, 1967
Loyter A, Schramm M: The glycogen-amylase complex as a means of obtaining highly purified α-amylases. Biochim Biophys Acta 65: 200–206, 1962
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ: Protein measurement with Folin Phenol reagent. J Biol Chem 193: 265–275,1951
Bernfeld P: Enzymes of starch degradation and synthesis. In: Nord FF (Ed) Advances in Enzymology. Interscience Pub. Inc. New York, London, Vol. 12, pp. 379–428, 1951
Chowdhury M, Sarkar M, Mandal C: Identification and isolation of an agglutinin from uterus of rats. Biochem Biophys Res Comm 130: 1301–1307, 1985
Levitzki A, Heller J, Schramm M: Specific precipitation of enzyme by its substrate: The α-amylase macrodextrin complex. Biochim Biophys Acta 81: 101–107, 1964
Ozanne B, Sambrook J: Binding of radioactivity labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells. Nature New Biol 232: 156–160, 1971
Hankins CN, Shannon LM: The physical and enzymatic properties of a phyto hemagglutinin from mung beans. J Biol Chem 253: 7791–7797, 1978.
Dey PM, Jones BMG, Naik S, Pridham JB: Binding of α-galactosidase I from Vicia faba to potato starch granules and sheep erythrocytes. Phytochem 23: 2169–2171, 1984
Roth S, White D: Intercellular contact and cell surface galactosyltransferase activity. Proc Nat Acad Sci USA 69: 485–489,1972
Shur BD: The receptor function of galactosyl transferase during cellular interactions. Mol Cell Biochem 61: 143–156, 1984
Banya EM, Runyan RB, Scully NF, Reichner J, Lopez LC, Shur BD. Cell surface galactosyl transferase as a recognition molecule during development. Mol Cell Biochem 72: 141–151,1986
International Union of Biochemistry: Nomenclature Committee: Arch Biochem Biophys 206: 458–462, 1981
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Begum, N., Chowdhury, M. Studies on the agglutinating activity of pancreatic extracts and its relevance to function. Mol Cell Biochem 108, 175–179 (1991). https://doi.org/10.1007/BF00233123