Heat-stable protein that stimulates acid alpha-glucosidase.

Journal: The Biochemical journal

Volume: 264

Issue: 3

Year of Publication: 1990

Affiliated Institutions:  Mental Health Research Institute, University of Michigan, Ann Arbor .

Abstract summary 

A hot-water extract of bovine spleen and guinea pig liver exhibited the ability to enhance acid alpha-glucosidase activity, with methylumbelliferyl alpha-glucoside, glycogen or maltose as substrate. The level of activator required for maximal stabilization was similar for all three substrates, indicating direct action on the enzyme rather than on substrate. The stimulator was partially purified by chromatography with gel-permeation (apparent Mr 20,000-24,000), ion-exchange and C4 reverse-phase columns. It was retained by a narrow-pore dialysis tubing and destroyed by treatment with Pronase, and is presumably a protein. The stimulating protein protected the enzyme against denaturation by heat or incubation with a buffer of high ionic strength in the absence of substrate. RNA inhibited the enzyme, and the activator protein was able to counteract the effect. Activating material was found in a variety of mouse and rat tissues, as well as human urine.

Authors & Co-authors:  Radin N S NS Shukla A A Shukla G S GS Sano A A

Study Outcome 

Source Link: Visit source

Statistics
Citations :  Pediatrics. 1968 Oct;42(4):672-6
Authors :  4
Identifiers
Doi : 
SSN : 0264-6021
Study Population
Male,Female
Mesh Terms
Animals
Other Terms
Study Design
Study Approach
Country of Study
Guinea
Publication Country
England