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Literature DB >> 1779963

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

Abstract

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.

Entities: Chemical Disease Species

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Year: 1991 PMID： 1779963 DOI： 10.1007/bf00233123

Source DB: PubMed Journal: Mol Cell Biochem ISSN： 0300-8177 Impact factor: 3.396

13 in total

1. The glycogen-amylase complex as a means of obtaining highly purified alpha-amylases.

Authors: A LOYTER; M SCHRAMM
Journal: Biochim Biophys Acta Date: 1962-12-04

2. The physical and enzymatic properties of a phytohemagglutinin from mung beans.

Authors: C N Hankins; L M Shannon
Journal: J Biol Chem Date: 1978-11-10 Impact factor: 5.157

3. Cell surface galactosyltransferase as a recognition molecule during development.

Authors: E M Bayna; R B Runyan; N F Scully; J Reichner; L C Lopez; B D Shur
Journal: Mol Cell Biochem Date: 1986 Nov-Dec Impact factor: 3.396

4. Binding of radioactively labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells.

Authors: B Ozanne; J Sambrook
Journal: Nat New Biol Date: 1971-08-04

5. Intercellular contact and cell-surface galactosyl transferase activity (cell culture-mouse-radioautography-contact inhibition-cis-and trans-galactosylation).

Authors: S Roth; D White
Journal: Proc Natl Acad Sci U S A Date: 1972-02 Impact factor: 11.205

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

1. The glycogen-amylase complex as a means of obtaining highly purified alpha-amylases.

2. The physical and enzymatic properties of a phytohemagglutinin from mung beans.

3. Cell surface galactosyltransferase as a recognition molecule during development.

4. Binding of radioactively labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells.

5. Intercellular contact and cell-surface galactosyl transferase activity (cell culture-mouse-radioautography-contact inhibition-cis-and trans-galactosylation).

6. Method for the isolation of intact islets of Langerhans from the rat pancreas.

7. Nomenclature. January 1981. Nomenclature Committee of IUB. IUB--IUPAC Joint Commission on Biochemical Nomenclature.

Review 8. The receptor function of galactosyltransferase during cellular interactions.

9. Identification and isolation of an agglutinin from uterus of rats.

10. Insulin release: reconciliation of the receptor and metabolic hypotheses. Nutrient receptors in islet cells.

1. Carbohydrate-binding profile of a pregnancy-associated rat uterine glycoprotein.