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

Department of Chemical and Materials Engineering

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

2 Scopus citations

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.

Original language	English
Title of host publication	Progress in Biotechnology
Publisher	Elsevier
Pages	59-62
Number of pages	4
Edition	C
DOIs	https://doi.org/10.1016/S0921-0423(00)80013-1
State	Published - 2000

Publication series

Name	Progress in Biotechnology
Number	C
Volume	16
ISSN (Print)	0921-0423

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10.1016/S0921-0423(00)80013-1

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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. In Progress in Biotechnology (C ed., pp. 59-62). (Progress in Biotechnology; Vol. 16, No. 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.",

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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. in Progress in Biotechnology. C edn, Progress in Biotechnology, no. C, vol. 16, Elsevier, pp. 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 et al.
Progress in Biotechnology. C. ed. Elsevier, 2000. p. 59-62 (Progress in Biotechnology; Vol. 16, No. C).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

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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