Study of Isothermal Adsorption of Bovine γGlobulin on Nylon Affinity Membrane with LTryptophane Ligand by Batch Method
- VernacularTitle:批量法研究牛γ-球蛋白在尼龙亲和膜上的等温吸附行为
- Author:
Hongyu GAN
;
Zhenhua SHANG
;
Xueliang LIU
;
Junde WANG
- Publication Type:Journal Article
- From:
Chinese Journal of Analytical Chemistry
2001;29(6):637-641
- CountryChina
- Language:Chinese
-
Abstract:
A new nylon affinity matrix with L-tryptoph ane as ligand was prepared for adsorption of bovine γ-globulin. Effects of tem perature, ionic strength and pH on affinity adsorption of γ-globulin on affinity membrane were studied by batch method. The results show that the interaction between ligand and γ-globulin includes mainly electrostatic and hydrophobic interaction. The affinity adsorption at optimum condition obeys Langmuir adsorption model with maximum adsorption capacity and minimum nonspecific adsorption. The space location between protein and ligand and the configuration of proteins wi ll change when deviating from this condition.
