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Comparative analysis of somatostatin analog peptides by capillary electrophoresis and micellar elektrokinetic chromatography.
Electrophoresis. 1996 Apr; 17(4):758-61.E

Abstract

Capillary electrophoresis (CE) and micellar electrokinetic chromatography (MEKC) methods, utilizing uncoated silica capillary and triethyl ammonium phosphate or sodium borate buffers in the pH range of 2.25-11.0, containing sodium dodecyl sulfate (SDS) (0-100 mM) for analysis of somatostatin-analog peptides were developed. The method presented here was compared with the reversed-phase high performance liquid chromatographic (RP-HPLC) and CE methods developed for analysis of peptides. The peptides investigated in this work can be separated by CE on the basis of their electrophoretic mobility in aqueous buffer of low pH value (pH 2.25) or by MEKC on the basis of their hydrophobicity in SDS containing buffer of high pH value (pH 11.0). Optimal MEKC separation of the investigated peptides has been achieved at pH 11.0 in an Na-borate buffer containing 100 mM SDS. CE at pH 2.25 proved insensitive to the hydrophobicity of the peptides investigated. By contrast, results obtained with MEKC at pH 11.0 proved to be anologous to those obtained by RP-HPLC, with highly hydrophobic peptides-migrating slower than peptides without hydrophobic moieties.

Authors+Show Affiliations

First Department of Biochemistry, Semmelweis University Medical School, Budapest, Hungary. MIKI@PUSKIN.SOTE.HUNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8738339

Citation

Idei, M, et al. "Comparative Analysis of Somatostatin Analog Peptides By Capillary Electrophoresis and Micellar Elektrokinetic Chromatography." Electrophoresis, vol. 17, no. 4, 1996, pp. 758-61.
Idei M, Mezö I, Vadász Z, et al. Comparative analysis of somatostatin analog peptides by capillary electrophoresis and micellar elektrokinetic chromatography. Electrophoresis. 1996;17(4):758-61.
Idei, M., Mezö, I., Vadász, Z., Horváth, A., Seprödi, J., Erchegyi, J., Teplán, I., & Kéri, G. (1996). Comparative analysis of somatostatin analog peptides by capillary electrophoresis and micellar elektrokinetic chromatography. Electrophoresis, 17(4), 758-61.
Idei M, et al. Comparative Analysis of Somatostatin Analog Peptides By Capillary Electrophoresis and Micellar Elektrokinetic Chromatography. Electrophoresis. 1996;17(4):758-61. PubMed PMID: 8738339.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comparative analysis of somatostatin analog peptides by capillary electrophoresis and micellar elektrokinetic chromatography. AU - Idei,M, AU - Mezö,I, AU - Vadász,Z, AU - Horváth,A, AU - Seprödi,J, AU - Erchegyi,J, AU - Teplán,I, AU - Kéri,G, PY - 1996/4/1/pubmed PY - 1996/4/1/medline PY - 1996/4/1/entrez SP - 758 EP - 61 JF - Electrophoresis JO - Electrophoresis VL - 17 IS - 4 N2 - Capillary electrophoresis (CE) and micellar electrokinetic chromatography (MEKC) methods, utilizing uncoated silica capillary and triethyl ammonium phosphate or sodium borate buffers in the pH range of 2.25-11.0, containing sodium dodecyl sulfate (SDS) (0-100 mM) for analysis of somatostatin-analog peptides were developed. The method presented here was compared with the reversed-phase high performance liquid chromatographic (RP-HPLC) and CE methods developed for analysis of peptides. The peptides investigated in this work can be separated by CE on the basis of their electrophoretic mobility in aqueous buffer of low pH value (pH 2.25) or by MEKC on the basis of their hydrophobicity in SDS containing buffer of high pH value (pH 11.0). Optimal MEKC separation of the investigated peptides has been achieved at pH 11.0 in an Na-borate buffer containing 100 mM SDS. CE at pH 2.25 proved insensitive to the hydrophobicity of the peptides investigated. By contrast, results obtained with MEKC at pH 11.0 proved to be anologous to those obtained by RP-HPLC, with highly hydrophobic peptides-migrating slower than peptides without hydrophobic moieties. SN - 0173-0835 UR - https://www.unboundmedicine.com/medline/citation/8738339/Comparative_analysis_of_somatostatin_analog_peptides_by_capillary_electrophoresis_and_micellar_elektrokinetic_chromatography_ L2 - https://doi.org/10.1002/elps.1150170422 DB - PRIME DP - Unbound Medicine ER -