Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein

Fu Yung Lin; Wen Yih Chen; Ruoh Chyu Ruaan; Hsiang Ming Huang

doi:10.1016/S0921-0423(00)80013-1

Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein

Fu Yung Lin, Wen Yih Chen, Ruoh Chyu Ruaan, Hsiang Ming Huang

化學工程與材料工程學系

研究成果: 書貢獻/報告類型 › 篇章 › 同行評審

2 引文斯高帕斯（Scopus）

摘要

Using Isothermal Titration Calorimetry (ITC), this investigation directly measured the adsorption enthalpies of proteins on various hydrophobic adsorbents. Various amounts of butyl and octyl groups were attached onto CM-Sepharose to form C4 and C8 two types of hydrophobic adsorbents. The adsorption enthalpies of both trypsingogen and α-chymotrypsinogen A were measured at 4.0 M NaCl and pH 10.0, in which most ionic interaction was suppressed. The adsorption isotherms of both proteins on various adsorbents were also measured thus allowing us to calculate the Gibbs free energy and entropy of adsorption.

原文	???core.languages.en_GB???
主出版物標題	Progress in Biotechnology
發行者	Elsevier
頁面	59-62
頁數	4
版本	C
DOIs	https://doi.org/10.1016/S0921-0423(00)80013-1
出版狀態	已出版 - 2000

出版系列

名字	Progress in Biotechnology
號碼	C
卷	16
ISSN（列印）	0921-0423

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10.1016/S0921-0423(00)80013-1

引用此

Lin, F. Y., Chen, W. Y., Ruaan, R. C., & Huang, H. M. (2000). Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein. 於 Progress in Biotechnology (C 編輯, 頁 59-62). (Progress in Biotechnology; 卷 16, 編號 C). Elsevier. https://doi.org/10.1016/S0921-0423(00)80013-1

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abstract = "Using Isothermal Titration Calorimetry (ITC), this investigation directly measured the adsorption enthalpies of proteins on various hydrophobic adsorbents. Various amounts of butyl and octyl groups were attached onto CM-Sepharose to form C4 and C8 two types of hydrophobic adsorbents. The adsorption enthalpies of both trypsingogen and α-chymotrypsinogen A were measured at 4.0 M NaCl and pH 10.0, in which most ionic interaction was suppressed. The adsorption isotherms of both proteins on various adsorbents were also measured thus allowing us to calculate the Gibbs free energy and entropy of adsorption.",

author = "Lin, {Fu Yung} and Chen, {Wen Yih} and Ruaan, {Ruoh Chyu} and Huang, {Hsiang Ming}",

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doi = "10.1016/S0921-0423(00)80013-1",

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Lin, FY, Chen, WY, Ruaan, RC & Huang, HM 2000, Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein. 於 Progress in Biotechnology. C edn, Progress in Biotechnology, 編號 C, 卷 16, Elsevier, 頁 59-62. https://doi.org/10.1016/S0921-0423(00)80013-1

Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein. / Lin, Fu Yung; Chen, Wen Yih; Ruaan, Ruoh Chyu 等.
Progress in Biotechnology. C. 編輯 Elsevier, 2000. p. 59-62 (Progress in Biotechnology; 卷 16, 編號 C).

研究成果: 書貢獻/報告類型 › 篇章 › 同行評審

TY - CHAP

T1 - Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography

T2 - effects of ligand chain length, density, and the amount of bound protein

AU - Lin, Fu Yung

AU - Chen, Wen Yih

AU - Ruaan, Ruoh Chyu

AU - Huang, Hsiang Ming

PY - 2000

Y1 - 2000

N2 - Using Isothermal Titration Calorimetry (ITC), this investigation directly measured the adsorption enthalpies of proteins on various hydrophobic adsorbents. Various amounts of butyl and octyl groups were attached onto CM-Sepharose to form C4 and C8 two types of hydrophobic adsorbents. The adsorption enthalpies of both trypsingogen and α-chymotrypsinogen A were measured at 4.0 M NaCl and pH 10.0, in which most ionic interaction was suppressed. The adsorption isotherms of both proteins on various adsorbents were also measured thus allowing us to calculate the Gibbs free energy and entropy of adsorption.

AB - Using Isothermal Titration Calorimetry (ITC), this investigation directly measured the adsorption enthalpies of proteins on various hydrophobic adsorbents. Various amounts of butyl and octyl groups were attached onto CM-Sepharose to form C4 and C8 two types of hydrophobic adsorbents. The adsorption enthalpies of both trypsingogen and α-chymotrypsinogen A were measured at 4.0 M NaCl and pH 10.0, in which most ionic interaction was suppressed. The adsorption isotherms of both proteins on various adsorbents were also measured thus allowing us to calculate the Gibbs free energy and entropy of adsorption.

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U2 - 10.1016/S0921-0423(00)80013-1

DO - 10.1016/S0921-0423(00)80013-1

M3 - 篇章

AN - SCOPUS:77957080624

T3 - Progress in Biotechnology

SP - 59

EP - 62

BT - Progress in Biotechnology

PB - Elsevier

ER -

Microcalorimetric studies of interactions between protein and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density, and the amount of bound protein

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