Detail of "54127-58-1"

Reference

Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand

All Rights Reserved. Protein adsorption kinetics of mixed-mode adsorbent with benzylamine as functional ligand. Gao, Dong; Lin, Dong-Qiang; Yao, Shan-Jing (Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027, Peop. Rep. China). Chemical Engineering Science, 61(22), 7260-7268 (English) 2006 Elsevier Ltd. CODEN: CESCAC. ISSN: 0009-2509. DOCUMENT TYPE: Journal CA Section: 66 (Surface Chemistry and Colloids) Section cross-reference(s): 6 Adsorption kinetics of bovine serum albumin (BSA) to mixed-mode adsorbent with benzylamine ligand was studied via stirred-batch uptake expts. The effects of liq.-phase conditions, such as salt concn. and pH, on the uptake rates of BSA were evaluated by effective pore diffusivity (De) derived from the pore diffusion model (PDM). The results indicated that when electrostatic attractive interactions exist between protein and ligand, De increases firstly with increasing salt concn. and then turns to decreasing after reaching the max. 54127-58-1 which is the cas registry number is also used here. When there are electrostatic repulsion protein/ligand interactions, it seems that the adsorption process is patch controlled, and the specific salt concn. to result in a min. adsorption capacity could be found. The value of D e showed a similar tendency to the change of adsorption capacities. With the increase of salt concn., the increase in De value was considered due to the decrease of electrostatic repulsion interactions and increase of hydrophobic interactions between BSA and ligand. Since BSA has the most compact structure at the isoelec. point, which leads to lower hydrodynamic forces, it is reasonable that the max. of effective diffusion coeff. could be found around the isoelec. point. .