Tryptophan and aliphatic side chain of amino acids adsorb onto aliphatic ligands through different driving forces

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Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/30577

Title:	Tryptophan and aliphatic side chain of amino acids adsorb onto aliphatic ligands through different driving forces
Authors:	Liu,C;Lin,PH;Lee,BF;Ruaan,RC
Contributors:	化學工程與材料工程研究所
Keywords:	PERFORMANCE LIQUID-CHROMATOGRAPHY;HYDROPHOBIC INTERACTION CHROMATOGRAPHY;PROTEIN-PROTEIN RECOGNITION;BOVINE SERUM-ALBUMIN;MONOMERIC PROTEINS;SURFACE;ADSORPTION;RESIDUES;THERMODYNAMICS;TEMPERATURE
Date:	2005
Issue Date:	2010-07-06 16:22:33 (UTC+8)
Publisher:	中央大學
Abstract:	The hydrophobic adsorption of three series of small peptides on commercial Octyl-Sepharose resins were investigated. The adsorption of tryptophan containing peptides was found to be driven by enthalpy. The enthalpy of adsorption on Octyl-Sepharose per try
Relation:	JOURNAL OF THE CHINESE INSTITUTE OF CHEMICAL ENGINEERS
Appears in Collections:	[National Central University Department of Chemical & Materials Engineering] journal & Dissertation

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