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Literature DB >> 2505756

Neutral maltase/glucoamylase from rabbit renal cortex.

Abstract

Maltase activity (EC 3.2.1.20) was solubilized from rabbit kidney brush-border membrane by using 1.0% Triton X-100 and purified 230-fold with an overall recovery of 30%. The purification procedure makes use of heat precipitation, chromatography on DE-52 DEAE-cellulose and gel filtration on Sephacryl S-300. Rabbit kidney brush border exhibited glucoamylase activity with a maltase/glucoamylase ratio of 1.5:1 to 2.0:1. During purification the maltase and glucoamylase activities behaved identically. The Mr of the complex is 590,000, and it appears to be composed of eight identical subunits linked by disulphide bridges.

Entities: Chemical Disease

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Year: 1989 PMID： 2505756 PMCID： PMC1138778 DOI： 10.1042/bj2610043

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

14 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

1 in total

Neutral maltase/glucoamylase from rabbit renal cortex.

1. Lowry determination of protein in the presence of Triton X-100.

2. METHOD FOR ASSAY OF INTESTINAL DISACCHARIDASES.

Review 3. Microvilli: their ultrastructure, enzymology and molecular organization.

4. Isolation and characterization of four forms of trehalase from rabbit kidney cortex.

5. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

6. Kidney brush border membrane maltase: purification and properties.

7. Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit.

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

9. Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney.

10. Kinetic studies on glucoamylase of rabbit small intestine.

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