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Evaluation of alumina-based stationary phases for the separations of proteins and peptides by high performance liquid chromatography

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Date Issued:
1991
Summary:
Alumina-based stationary phases are evaluated for the separations of proteins and peptides by reversed phase high performance liquid chromatography. Separations are compared to those obtained on a widely-used octadecylsilane (ODS) phase. The separations of peptides on alumina-based stationary phases are found to be superior while separations of proteins are inferior as compared to those found on ODS phase. The superior performance of peptide separations on alumina-based columns is attributed to lower pore size and uniquely-shaped particles of the alumina. The retentions of peptides and proteins on both alumina and silica-based stationary phases are shown to be governed by hydrophobic interaction mechanisms.
Title: Evaluation of alumina-based stationary phases for the separations of proteins and peptides by high performance liquid chromatography.
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Name(s): Raghani, Anil Ratilal.
Florida Atlantic University, Degree grantor
Haky, Jerome E., Thesis advisor
Type of Resource: text
Genre: Electronic Thesis Or Dissertation
Issuance: monographic
Date Issued: 1991
Publisher: Florida Atlantic University
Place of Publication: Boca Raton, Fla.
Physical Form: application/pdf
Extent: 117 p.
Language(s): English
Summary: Alumina-based stationary phases are evaluated for the separations of proteins and peptides by reversed phase high performance liquid chromatography. Separations are compared to those obtained on a widely-used octadecylsilane (ODS) phase. The separations of peptides on alumina-based stationary phases are found to be superior while separations of proteins are inferior as compared to those found on ODS phase. The superior performance of peptide separations on alumina-based columns is attributed to lower pore size and uniquely-shaped particles of the alumina. The retentions of peptides and proteins on both alumina and silica-based stationary phases are shown to be governed by hydrophobic interaction mechanisms.
Identifier: 14719 (digitool), FADT14719 (IID), fau:11510 (fedora)
Note(s): Charles E. Schmidt College of Science
Thesis (M.S.)--Florida Atlantic University, 1991.
Subject(s): Proteins--Separation
High performance liquid chromatography
Held by: Florida Atlantic University Libraries
Persistent Link to This Record: http://purl.flvc.org/fcla/dt/14719
Sublocation: Digital Library
Use and Reproduction: Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder.
Use and Reproduction: http://rightsstatements.org/vocab/InC/1.0/
Host Institution: FAU
Is Part of Series: Florida Atlantic University Digital Library Collections.