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Data for semi-permanent cationic coating for protein separations
Protein separations and analyses are fundamental to fields of study that include biochemistry, biology, physiology, drug discovery, pharmaceuticals, as well as agricultural and food based industries. Here, we provide the data from a novel phospholipid-cetyltrimethylammonium bromide coating capable o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7186883/ https://www.ncbi.nlm.nih.gov/pubmed/32368572 http://dx.doi.org/10.1016/j.dib.2020.105123 |
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author | Crihfield, C.L. Kristoff, C.J. Veltri, L.M. Wilson, C.A. Penny, W.M. Holland, L.A. |
author_facet | Crihfield, C.L. Kristoff, C.J. Veltri, L.M. Wilson, C.A. Penny, W.M. Holland, L.A. |
author_sort | Crihfield, C.L. |
collection | PubMed |
description | Protein separations and analyses are fundamental to fields of study that include biochemistry, biology, physiology, drug discovery, pharmaceuticals, as well as agricultural and food based industries. Here, we provide the data from a novel phospholipid-cetyltrimethylammonium bromide coating capable of separating cationic and anionic proteins with high efficiency. Capillary electrophoresis separations of protein standards were utilized to characterize the performance of the novel coating. Using capillary electrophoresis with UV absorbance detection a working pH range of 4–9 was identified, with reproducibility in time ≤1% relative standard deviation, and plate counts for proteins as high as 480,000 plates (lysozyme, pH 7). Further details and results from these data are available in the work reported by Crihfield et al. and can be accessed at https://doi.org/10.1016/j.chroma.2019.460397 [1]. |
format | Online Article Text |
id | pubmed-7186883 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-71868832020-05-04 Data for semi-permanent cationic coating for protein separations Crihfield, C.L. Kristoff, C.J. Veltri, L.M. Wilson, C.A. Penny, W.M. Holland, L.A. Data Brief Chemistry Protein separations and analyses are fundamental to fields of study that include biochemistry, biology, physiology, drug discovery, pharmaceuticals, as well as agricultural and food based industries. Here, we provide the data from a novel phospholipid-cetyltrimethylammonium bromide coating capable of separating cationic and anionic proteins with high efficiency. Capillary electrophoresis separations of protein standards were utilized to characterize the performance of the novel coating. Using capillary electrophoresis with UV absorbance detection a working pH range of 4–9 was identified, with reproducibility in time ≤1% relative standard deviation, and plate counts for proteins as high as 480,000 plates (lysozyme, pH 7). Further details and results from these data are available in the work reported by Crihfield et al. and can be accessed at https://doi.org/10.1016/j.chroma.2019.460397 [1]. Elsevier 2020-01-11 /pmc/articles/PMC7186883/ /pubmed/32368572 http://dx.doi.org/10.1016/j.dib.2020.105123 Text en © 2020 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Chemistry Crihfield, C.L. Kristoff, C.J. Veltri, L.M. Wilson, C.A. Penny, W.M. Holland, L.A. Data for semi-permanent cationic coating for protein separations |
title | Data for semi-permanent cationic coating for protein separations |
title_full | Data for semi-permanent cationic coating for protein separations |
title_fullStr | Data for semi-permanent cationic coating for protein separations |
title_full_unstemmed | Data for semi-permanent cationic coating for protein separations |
title_short | Data for semi-permanent cationic coating for protein separations |
title_sort | data for semi-permanent cationic coating for protein separations |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7186883/ https://www.ncbi.nlm.nih.gov/pubmed/32368572 http://dx.doi.org/10.1016/j.dib.2020.105123 |
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