Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Kinetic studies on glucoamylase of rabbit small intestine.

Literature DB >> 6006

Kinetic studies on glucoamylase of rabbit small intestine.

Abstract

The kinetic properties of a maltase-glucoamylase complex with a neutral pH optimum, purified to homogeneity from the brush borders of the rabbit small intestine, are described. It has a broad range of substrate specificity, hydrolysing di- and poly-saccharides with alpha-1,4 and alpha-1,6 linkages. The Km and Vmax, values of the enzyme for the various substrates were determined. Starch and maltose were its best substrates. The kinetics of hydrolysis of two synthetic linear maltosaccharides, namely maltotriose and maltopentaose, were studied. Mixed-substrate incubation studies revealed the presence of at least two interacting sites on the enzyme, and the data were further analysed by the use of a number of non-substrate inhibitors.

Entities: Chemical

Mesh：

Substances：

Year: 1976 PMID： 6006 PMCID： PMC1172577 DOI： 10.1042/bj1530321

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.766

17 in total

1. STUDIES ON LIVER ALCOHOL HYDROGENASE COMPLEXES. 3. MULTIPLE INHIBITION KINETICS IN THE PRESENCE OF TWO COMPETITIVE INHIBITORS.

Authors: T YONETANI; H THEORELL
Journal: Arch Biochem Biophys Date: 1964-07-20 Impact factor: 4.013

2. Tissue fractionation studies. 16. Intracellular distribution and properties of alpha-glucosidases in rat liver.

Authors: N LEJEUNE; D THINES-SEMPOUX; H G HERS
Journal: Biochem J Date: 1963-01 Impact factor: 3.857

3. Protein measurement with the Folin phenol reagent.

Authors: O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal: J Biol Chem Date: 1951-11 Impact factor: 5.157

4. Enzymatic properties of rat lactase-phlorizin hydrolase.

Authors: E Birkenmeier; D H Alpers
Journal: Biochim Biophys Acta Date: 1974-05-20

5. Studies on intestinal disaccharidases. V. Characterization and properties of maltase fractions from monkey intestine.

Authors: N Swaminathan; A N Radhakrishnan
Journal: Indian J Biochem Date: 1970-03

6. Steady-state kinetics of rabbit-intestinal sucrase. Kinetic mechanism, Na+ activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite.

Authors: G Semenza; A K von Balthazar
Journal: Eur J Biochem Date: 1974-01-03

7. Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200.

Authors: S Sivakami; A N Radhakrishnan
Journal: Indian J Biochem Biophys Date: 1973-12 Impact factor: 1.918

8. The preparation of lactase and glucoamylase of rat small intestine.

Authors: S Schlegel-Haueter; P Hore; K R Kerry; G Semenza
Journal: Biochim Biophys Acta Date: 1972-02-28

9. Lactase-phlorizin hydrolase complex from monkey small intestine: stimulation of phlorizin hydrolase activity by organic acids.

Authors: S Ramaswamy; A N Radhakrishnan
Journal: Biochem Biophys Res Commun Date: 1973-09-05 Impact factor: 3.575

10. Studies on mammalian glucoamylases with special reference to monkey intestinal glucoamylase.

Authors: B Seetharam; N Swaminathan; A N Radhakrishnan
Journal: Biochem J Date: 1970-05 Impact factor: 3.857

8 in total

1. A comparison of the active site of maltase-glucoamylase from the brush border of rabbit small intestine and kidney by chemical modification studies.

Authors: B Pereira; S Sivakami
Journal: Biochem J Date: 1991-03-01 Impact factor: 3.857

Kinetic studies on glucoamylase of rabbit small intestine.

1. STUDIES ON LIVER ALCOHOL HYDROGENASE COMPLEXES. 3. MULTIPLE INHIBITION KINETICS IN THE PRESENCE OF TWO COMPETITIVE INHIBITORS.

2. Tissue fractionation studies. 16. Intracellular distribution and properties of alpha-glucosidases in rat liver.

3. Protein measurement with the Folin phenol reagent.

4. Enzymatic properties of rat lactase-phlorizin hydrolase.

5. Studies on intestinal disaccharidases. V. Characterization and properties of maltase fractions from monkey intestine.

6. Steady-state kinetics of rabbit-intestinal sucrase. Kinetic mechanism, Na+ activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite.

7. Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200.

8. The preparation of lactase and glucoamylase of rat small intestine.

9. Lactase-phlorizin hydrolase complex from monkey small intestine: stimulation of phlorizin hydrolase activity by organic acids.

10. Studies on mammalian glucoamylases with special reference to monkey intestinal glucoamylase.

1. A comparison of the active site of maltase-glucoamylase from the brush border of rabbit small intestine and kidney by chemical modification studies.

2. α-glucosidase from grape berries: Partial purification and characterization.

3. Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH.

4. Enzyme activity in partly dissociated fragments of rat intestinal maltase/glucoamylase.

5. Neutral maltase/glucoamylase from rabbit renal cortex.

6. Thermostable glucose-tolerant glucoamylase produced by the thermophilic fungus Scytalidium thermophilum.

7. Studies on the size and shape of rabbit intestinal glucoamylase-maltase complex.

8. Purification and properties of neutral maltase from human granulocytes.