Micellar Electrokinetic Chromatographic Separation of Basic Polypeptides with Equal Mass to Charge Ratio Using Dynamically Modified Silica Capillaries

Kristensen, Helle Kjærgaard; Hansen, Steen Honoré

doi:10.1080/10826079308019626

Cited by 14 publications

(1 citation statement)

References 15 publications

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“…Several attempts have been taken to eliminate or reduce solute-wall interactions Among them are: (a) capillary wall modifications [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24]; (b) control of the pH and ionic strength of the run buffer [25][26][27][28][29]; (c) use of non-ionic or zwitterionic buffers or buffer additives [30][31][32][33][34][35][36][37]; and (d) use of an additional radial electric field [38]. Capillary wall modification has proven to be the most versatile method for the separation of proteins, but short capillary lifetime is often a drawback.…”

Section: Introductionmentioning

confidence: 99%

Capillary zone electrophoretic separation of basic proteins and drugs using guaran as a buffer modifier

Liu

Lin

Hartwick³

1998

Chromatographia

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SummaryGuaran, a neutral polysaccharide, has been used as a buffer modifier to improve the separation of basic proteins and drugs. Migration reproducibility, peak shape and efficiency were improved when 0.1% guaran was added to the buffer. The concentration of guaran, ionic strength, and pH of buffer solution were optimized to obtain the optimum separation of proteins. Possible separation efficiencies of 700,000 plates per meter were obtained for test proteins. The relative standard deviation (%RSD) of the migration time of all test proteins was less than 0.5 %. Improved separation of [3-blockers was also observed when guaran was added to the buffer.

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Section: Introductionmentioning

confidence: 99%

Capillary zone electrophoretic separation of basic proteins and drugs using guaran as a buffer modifier

Liu

Lin

Hartwick³

1998

Chromatographia

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Separation of eleven angiotensin II analogs by capillary electrophoresis with a nonionic surfactant in acidic media

Matsubara¹,

Koezuka²,

Terabe³

1995

Electrophoresis

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Eleven angiotension II analogs of same chain length were separated by capillary electrophoresis at pH 2.0 with 200 mM Tween 20. All compounds except one pair of angiotensin II ([Sar1, Gly8]- and [Sar1, Val5, Ala8]-angiotensin II) were baseline-separated, even in the case of peptides with about the same total charge. The migration order of the angiotensin II analogs were determined by the hydrophobicity of the amino acid as long as the difference between amino acids of two peptides is the conservative change. From the study of pH dependency of the separation of these peptides, it was found that the conditions of a low electroosmotic flow under a low pH is effective for the separation of similar peptides.

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Capillary zone electrophoresis and micellar electrokinetic chromatography, with taurodeoxycholate as micellar agent, of protein kinase A peptide substrates

Beijersten

Westerlund

1996

Electrophoresis

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The separation of protein kinase A peptide substrates with the general formula -X-Arg-Arg-Ala-Ser-Y-, where X and Y may be the same or different amino acids, was studied by capillary zone electrophoresis (CZE) and micellar electrokinetic chromatography (MEKC). Taurodeoxycholate (TDC) was used as the micellar agent. CZE was effective in separating a peptide series differing in the number of amino acids, but not for a series with a difference in the terminating amino acid. For the latter series, MEKC generally gave a higher selectivity, but some of the peptide pairs were more easily separated by CZE, demonstrating the complementary character of the two techniques. The efficiency of the MEKC system was typically < 50% of that of CZE, but its higher selectivity generally outbalanced the lower efficiency regarding resolution. The distribution of the peptides to the micelles was studied by determination of retention factors. Electrostatic and hydrophobic forces were found to be determining factors in the distribution; the most highly charged basic peptides were most heavily distributed, and for peptides with the same charge those containing more hydrophobic amino acids were more strongly distributed. The contribution of some structural features to the distribution degree was also determined.

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Micellar Electrokinetic Chromatographic Separation of Basic Polypeptides with Equal Mass to Charge Ratio Using Dynamically Modified Silica Capillaries

Cited by 14 publications

References 15 publications

Capillary zone electrophoretic separation of basic proteins and drugs using guaran as a buffer modifier

Capillary zone electrophoretic separation of basic proteins and drugs using guaran as a buffer modifier

Separation of eleven angiotensin II analogs by capillary electrophoresis with a nonionic surfactant in acidic media

Capillary zone electrophoresis and micellar electrokinetic chromatography, with taurodeoxycholate as micellar agent, of protein kinase A peptide substrates

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