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Comparison of alkyl-bonded alumina-based stationary phases for peptide separation by high performance liquid chromatography

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Date Issued:
1992
Summary:
The performance of several alkyl-bonded alumina-based stationary phases was evaluated by comparing the separation of synthetic octapeptide and polypeptide mixtures and tryptic digests of larger proteins. These phases were of differing pore diameter, alkyl chain length modification and particle shape and size. The separations were compared to standard silica phases. The narrow pore octadecyl bonded alumina phase outperformed the other alumina and silica phases in terms of separation efficiency and mobile phase resistance. Superior performance is attributed to the enhanced solute mass transfer properties and the unique morphology of the microplatelet alumina particles. The mechanism of separation gradually changes with increasing size of the peptide.
Title: Comparison of alkyl-bonded alumina-based stationary phases for peptide separation by high performance liquid chromatography.
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Name(s): Ramdial, Nirmala Debra-Ann
Florida Atlantic University, Degree Grantor
Haky, Jerome E., Thesis advisor
Department of Chemistry and Biochemistry
Charles E. Schmidt College of Science
Type of Resource: text
Genre: Electronic Thesis Or Dissertation
Issuance: monographic
Date Issued: 1992
Publisher: Florida Atlantic University
Place of Publication: Boca Raton, Fla.
Physical Form: application/pdf
Extent: 157 p.
Language(s): English
Summary: The performance of several alkyl-bonded alumina-based stationary phases was evaluated by comparing the separation of synthetic octapeptide and polypeptide mixtures and tryptic digests of larger proteins. These phases were of differing pore diameter, alkyl chain length modification and particle shape and size. The separations were compared to standard silica phases. The narrow pore octadecyl bonded alumina phase outperformed the other alumina and silica phases in terms of separation efficiency and mobile phase resistance. Superior performance is attributed to the enhanced solute mass transfer properties and the unique morphology of the microplatelet alumina particles. The mechanism of separation gradually changes with increasing size of the peptide.
Identifier: 14831 (digitool), FADT14831 (IID), fau:11619 (fedora)
Note(s): Charles E. Schmidt College of Science
Thesis (M.S.)--Florida Atlantic University, 1992.
Subject(s): Peptides--Separation
Liquid chromatography
Held by: Florida Atlantic University Libraries
Persistent Link to This Record: http://purl.flvc.org/fcla/dt/14831
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.