Contents Menu

Studies on the Carbohydrate-Binding Specificity of Glycogen Phosphorylases by Means of Affinity Electrophoresis

山口医学 Volume 34 Issue 4 Page 319-330
published_at 1985-08
Title
親和電気泳動法によるグリコーゲン・ホスホリラーゼの糖結合特性の研究
Studies on the Carbohydrate-Binding Specificity of Glycogen Phosphorylases by Means of Affinity Electrophoresis
Creators Suzuki Isao
Source Identifiers
Dissociation constans of rabbit muscle glycogen phosphorylases for various carbohydrates were measured by affinity electrophoresis. 1. Dissociation constants for glycogen at 5℃ was about one five-hundredth of that at 42.5℃. In other words, affinity of phosphorylase for glycogen at 5℃ was approximately 500 times stronger than that at 42.5℃. 2. Thermodynamic constants (△H^。 and △S^。) were calculated from the van't Hoff plots. The results indicated that the interaction between phosphorylase and glycogen was an exothermic reaction and the enzyme became of more ordered conformation. 3. The size of the carbohydrate-binding site of phosphorylase corresponds to that of maltohexaose. Cyclic maltose-type oligosaccharides competed with glycogen for the carbohydrate-binding site of phosphorylase. 4. All of the results mentioned above were quite similar for both phosphorylases a and b. From these results, it is concluded that glycogen and maltose-type oligosaccharides bind to phosphorylase at the glycogen storage site, and this site exists independently of the catalytic site and the AMP-binding site.
Subjects
医学 ( Other)
Languages jpn
Resource Type journal article
Publishers 山口大学医学会
Date Issued 1985-08
File Version Not Applicable (or Unknown)
Access Rights metadata only access
Relations
[ISSN]0513-1731
[NCID]AN00243156
Schools 医学部