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Modification of the selectivity of a reversed-phase high-performance liquid chromatographic system by binding sodium dodecyl sulphate to peptides

✍ Scribed by L.Dalla Libera


Book ID
104145601
Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
286 KB
Volume
507
Category
Article
ISSN
1873-3778

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✦ Synopsis


Cytochrome c and myoglobin were subjected to sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis, electroeluted from the gel and fragmentated with cyanogen bromide. High-performance liquid chromatographic (HPLC) separation of the peptide mixtures obtained was improved when using a gradient of acetonitrile containing phosphates in comparison with a gradient containing trifluoroacetic acid. This finding may be useful for the HPLC analysis of peptides derived from SDSprotein complexes.


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