Peptide mapping by capillary electrophoresis with Pluronic F127
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| Title: | Peptide mapping by capillary electrophoresis with Pluronic F127 |
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| Authors: | Mikšík, Ivan miksik@biomed.cas.cz, Charvátová, Jana1, Eckhardt, Adam1, Deyl, Zdeněk1 |
| Source: | Journal of Chromatography B: Analytical Technologies in the Biomedical & Life Sciences. Feb2004, Vol. 800 Issue 1/2, p155. 6p. |
| Subjects: | Peptides, Proteins, Capillary electrophoresis, Phosphates, Separation (Technology) |
| Abstract: | Separation of peptides and proteins by capillary zone electrophoresis suffers from the interaction of these solutes with the capillary wall which results in the formation of broad peaks and low resolution. To minimize the protein/peptide–capillary wall interaction we tried to use Pluronic F127, a triblock copolymer of the general formula (polyethylene oxide)x(polypropylene oxide)y(polyethylene oxide)z when |
| Copyright of Journal of Chromatography B: Analytical Technologies in the Biomedical & Life Sciences is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 11729385 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Peptide mapping by capillary electrophoresis with Pluronic F127 – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Mikšík%2C+Ivan%22">Mikšík, Ivan</searchLink><i> miksik@biomed.cas.cz</i><br /><searchLink fieldCode="AR" term="%22Charvátová%2C+Jana%22">Charvátová, Jana</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Eckhardt%2C+Adam%22">Eckhardt, Adam</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Deyl%2C+Zdeněk%22">Deyl, Zdeněk</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Chromatography+B%3A+Analytical+Technologies+in+the+Biomedical+%26+Life+Sciences%22">Journal of Chromatography B: Analytical Technologies in the Biomedical & Life Sciences</searchLink>. Feb2004, Vol. 800 Issue 1/2, p155. 6p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Capillary+electrophoresis%22">Capillary electrophoresis</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphates%22">Phosphates</searchLink><br /><searchLink fieldCode="DE" term="%22Separation+%28Technology%29%22">Separation (Technology)</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Separation of peptides and proteins by capillary zone electrophoresis suffers from the interaction of these solutes with the capillary wall which results in the formation of broad peaks and low resolution. To minimize the protein/peptide–capillary wall interaction we tried to use Pluronic F127, a triblock copolymer of the general formula (polyethylene oxide)x(polypropylene oxide)y(polyethylene oxide)z when <F>x=106</F>, <F>y=70</F> and <F>z=106</F> which can be considered a surfactant capable of self-association both into isotropic and anisotropic gels. The analytes studied were enzymatic digests (obtained by trypsin or pepsin treatment) of insoluble matrix proteins from avian eggshell. The best separations were obtained by a system exploiting 10% Pluronic F127 in 20 mmol/l phosphate buffer, pH 2.5. Electrophoretic peptide profiles obtained were very complex owing to the complicated nature of the samples (the exact composition of the proteinous insoluble part of the eggshell is still unknown). The separation in phosphate buffer only offered complex maps of incompletely resolved peaks. The use of Pluronic F127 distinctly improved the separation with a considerably better resolution regarding both the number of peaks obtained and the quality of the separation. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Chromatography B: Analytical Technologies in the Biomedical & Life Sciences is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.jchromb.2003.09.012 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 6 StartPage: 155 Subjects: – SubjectFull: Peptides Type: general – SubjectFull: Proteins Type: general – SubjectFull: Capillary electrophoresis Type: general – SubjectFull: Phosphates Type: general – SubjectFull: Separation (Technology) Type: general Titles: – TitleFull: Peptide mapping by capillary electrophoresis with Pluronic F127 Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Mikšík, Ivan – PersonEntity: Name: NameFull: Charvátová, Jana – PersonEntity: Name: NameFull: Eckhardt, Adam – PersonEntity: Name: NameFull: Deyl, Zdeněk IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 02 Text: Feb2004 Type: published Y: 2004 Identifiers: – Type: issn-print Value: 15700232 Numbering: – Type: volume Value: 800 – Type: issue Value: 1/2 Titles: – TitleFull: Journal of Chromatography B: Analytical Technologies in the Biomedical & Life Sciences Type: main |
| ResultId | 1 |