A mixture of 12 angiotensins was separated by high-performance liquid chromatography on a weak anion-exchange bonded phase using a triethylammonium acetate buffer and acetonitrile as the eluant. An excellent separation of these compounds was obtained. Recoveries for all 12 were over 90%, as determin
Separation and purification of diastereomers of angiotensin I by weak anion-exchange high-performance liquid chromatography
โ Scribed by Sam A. Margolis; Miral Dizdaroglu
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 745 KB
- Volume
- 322
- Category
- Article
- ISSN
- 1873-3778
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โฆ Synopsis
Several diastereomers of angiotensin I were resolved by weak anion-exchange high-performance liquid chromatography (HPLC). All of the diastereomers which were examined contained significant amounts of peptides whose amino acid composition differed from the designated diastereomer of angiotensin I. The des-Asp' forms of angiotensin I and the impurities were weakly retained on the anion-exchange column and were well separated from the rest of the peptides. Many of the impurities contained fractional amounts of amino acids suggesting that peptides which contained variable amounts of histidine and arginine are not resolved by this method. The results are compared with the results of separations of the same peptides by reversed-phase HPLC. This comparison strongly suggests that the two HPLC methods, utilizing different separation principles, are complementary; hence their combined use leads to a more confident assessment of the purity of a given peptide preparation.
๐ SIMILAR VOLUMES
## All naturally occurring sphingomyelins have the D-erythro-(2S,3R ) configuration of the sphingoid base. We have developed a normal-phase HPLC method for the separation of this natural stereoisomer from the L- threo-sphingomyelin, which is the other stereoisomer commonly present in semisynthetic