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Determination of binding constants of human insulin complexes with serotonin, dopamine, arginine, and phenol by pressure assisted partial filling affinity capillary electrophoresis
Šolínová, Veronika ; Žáková, Lenka ; Jiráček, Jiří ; Kašička, Václav
A new method, pressure assisted partial filling affinity capillary electrophoresis (PF-ACE), has been developed to study noncovalent interactions of the hexamer of human insulin (HI) with cationic ligands, such as phenolic neurotransmitters serotonin and dopamine, and amino acid arginine, or with anionic ligand phenol, in alkaline aqueous solutions. The apparent binding constants, Kb, of the HI-ligand complexes were determined from the dependence of the effective migration time changes of the above ligands on the variable zone lengths of HI dissolved in the background electrolyte and hydrodynamically introduced into the bare fused silica capillary close to the UV detector. The HI interactions with the above ligands were found to be moderately strong, with Kb values in the range 385-1314 L/mol.
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New semisynthetic analogs of human insulin
Škarda, Josef ; Barth, T. ; Velek, Jiří ; Barthová, J. ; Ježek, J. ; Huml, K. ; Kašička, V. ; Ubik, K. ; Velková, V. ; Hauzerová, L. ; Nováková, M. ; Klasová, L. ; Zórad, Š.
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Preparation and characterization of analogs of tetrapeptide B 23 -B 26 and octapeptide B 23 -B 30 of human insulin
Ježek, Jan ; Velek, Jiří ; Velková, Vlasta ; Klasová, L. ; Barthová, J. ; Ubik, Karel ; Kašička, Václav ; Barth, Tomislav ; Wollmer, A. ; Huml, Karel ; Hauzerová, Linda ; Brandenburg, D.
Gly-Phe-Phe-PheNH2, Gly-Phe-Phe-N(Me)Phe-NH2, Gly-Phe-N(Me)Phe-Phe-NH2, and Gly-Phe-Phe-N(Me)Tyr-NH2 and octapeptides Gly-Phe-Phe-N(Me)Phe-Thr-Pro-Lys(Pac)-Thr-OH and Gly-Phe-Phe-Phe-Thr-Pro-Lys(Pac)-Thr-OH. The compounds were isolated by preparative HPLC and characterized by amino acid analysis.
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