Study of Isothermal Adsorption of Bovine γGlobulin on Nylon Affinity Membrane with LTryptophane Ligand by Batch Method / 分析化学
Chinese Journal of Analytical Chemistry
;
(12): 637-641, 2001.
Artículo
en Chino
| WPRIM
| ID: wpr-410239
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.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Idioma:
Chino
Revista:
Chinese Journal of Analytical Chemistry
Año:
2001
Tipo del documento:
Artículo
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