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Evaluation of alumina-based stationary phases for the separations of proteins and peptides by high performance liquid chromatography
- 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 |
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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. |
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Subject(s): |
Proteins--Separation High performance liquid chromatography |
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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. |