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Enzymatic Hydrolysis of Disaccharide Unit of Collagen. Isolation of 2-O-alpha-d-Glucopyranosyl-O-beta-d-galactopyranosyl-hydroxylysine Glucohydrolase from Rat Spleens
- Source :
- European Journal of Biochemistry. 111:587-591
- Publication Year :
- 1980
- Publisher :
- Wiley, 1980.
-
Abstract
- The hydroxylsine-linked disaccharide unit, 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine (Glc-Gal-Hyl), prepared from collagens, was hydrolyzed by a glucohydrolase present in rat spleens and lungs. This disaccharide unit was scarcely hydrolyzed by homogenates of intestines, livers, and kidneys, which had a high alpha-D-glucosidase activity for neutral glucosides. The Glc-Gal-Hyl glucohydrolase was purified from rat spleens by affinity chromatography and gel filtration to the extent that sodium dodecyl sulfate/polyacrylamide gel electrophoresis gave a single band stained by Coomassie blue G-250. This purified glucohydrolase had a pH optimum around 5.8, and the Michaelis constant was 5.9 mM when Glc-Gal-Hyl was used as a substrate. This enzyme did not hydrolyze neutral glucosides. It is concluded that this Glc-Gal-Hyl glucohydrolase is responsible for catabolism of the hydroxylsine-linked disaccharide unit derived from collagens in mammals.
- Subjects :
- Male
Cations, Divalent
Size-exclusion chromatography
Disaccharide
Disaccharides
Biochemistry
Substrate Specificity
chemistry.chemical_compound
Hydrolysis
Affinity chromatography
Enzymatic hydrolysis
Animals
Tissue Distribution
Sodium dodecyl sulfate
Polyacrylamide gel electrophoresis
Chromatography
integumentary system
Rats
carbohydrates (lipids)
Kinetics
Hydroxylysine
chemistry
Collagen
Glucosidases
Spleen
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 111
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....bbcd6deab39d280030b9c50a488ed7e2