Influence of electrostatic interactions and enzyme reactivity on the binding mode of alpha-amylase
✍ Scribed by Engin Çörüşlü; Burhan Peki̇n
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 434 KB
- Volume
- 127
- Category
- Article
- ISSN
- 0008-6215
No coin nor oath required. For personal study only.
✦ Synopsis
Alpha-amylase was coupled to cellulose and carboxymethylcellulose through activation with cyanogen bromide. The specific activities, retentions of native enzyme activity, and action patterns of the resulting immobilised derivatives depended markedly on the pH of the coupling reaction. This dependency is discussed in terms of the role of the coupling pH in the regulation of electrostatic interactions and enzyme reactivity.
📜 SIMILAR VOLUMES
The enantioselectivities of subtilisin Carlsberg and Rhizomucor miehei lipase in organic solvents are found to strongly depend on the method by which the enzymes are prepared. For the transesterification between sec- phenethyl alcohol and vinyl butyrate in dioxane at 7"C, the enantioselectivity of s
## Abstract Inhibition of the enzyme catechol __O__‐methyltransferase (COMT) is of significant interest in the therapy of __Parkinson__'s disease. Described herein are structural analogs of the potent bisubstrate inhibitor (−)‐1 (__IC__~50~=9 nM; __Table 1__) for COMT, with target modifications of
Affinity chromatography provides a powerful tool for isolation of carbohydrate-binding proteins. However, the choice of the ligand and spacer has an important impact on effectiveness. The influence of several different ligands on qualitative and quantitative aspects of the purification of two beta-g