Národní úložiště šedé literatury Nalezeno 105 záznamů.  začátekpředchozí96 - 105  přejít na záznam: Hledání trvalo 0.00 vteřin. 
Separation of peptides by capillary zone electrophoresis with regulation of electroosmotic flow by radial electric field
Kašička, Václav ; Prusík, Zdeněk ; Sázelová, Petra ; Koval, Dušan ; Barth, Tomislav ; Brynda, Eduard ; Stejskal, Jaroslav
A new way of control of efficiency, resolution and speed of peptide separations by capillary zone electrophoresis based on the regulation of electroosmotic flow by radial electric field has been developed.
Effect of .I.N./I.-methylation of the peptide bond in the C-terminal part of the B-chain of human insulin on biological activity
Klasová, Lenka ; Zórad, Š. ; Velek, Jiří ; Ježek, Jan ; Kašička, Václav ; Barthová, J. ; Barth, Tomislav
Affinity of six analogs of human insulin to insulin receptors in rat adipose tissue and their ability to stimulate the transport of 2-deoxy-D-1 3 H-glucose into isolated rat adipocytes was determined.
Qualitative and quantitative microanalysis and preparative purification of biopeptides by capillary and continuous free-flow electrophoresis
Kašička, Václav ; Prusík, Zdeněk ; Sázelová, Petra ; Ježek, Jan ; Jiráček, Jiří ; Hlaváček, Jan ; Velek, Jiří ; Barth, Tomislav
High-performance capillary electrophoresis (HPCE) has been applied to qualitative and quantitative analysis of several biologically active peptides and their derivatives and fragments, e.g. insulins, insect oostatic hormones, and peptide and glycopeptide dendrimers.
Side reactions during photochemical cleavage of ŕ-methyl-6-nitroveratryl-based photolabile linker
Rinnová, Markéta ; Collinsová, Michaela ; Kašička, Václav ; Jiráček, Jiří
We have identified significant side reactions using ŕ-methyl-6-nitroveratryl-based photolinker for study of biological interactions.
Desoctapeptideinsulin: Substrate of ŕ-chymotrypsin
Koubová, V. ; Barthová, J. ; Barth, Tomislav ; Bezouška, K. ; Ubik, Karel ; Kašička, Václav
Desoctapeptideinsulin (DOI) contains three tyrosine residues and therefore it represents a suitable substrate for ŕ-chymotrypsin. The detailed enzymic study reveated a series of intermediates and final products. The bonds formed by tyrosine A14 and B16 are attacked as the first, and the products are further desintagrated.
Desoctapeptideinsulin fragments formed by chymotryptic cleavage and suitable for modification of insulin in positions A 14 and B 16
Koubová, V. ; Barthová, J. ; Kašička, Václav ; Ubik, Karel ; Barth, Tomislav ; Bezouška, K.
The molecule of desoctapeptide insulin is cleaved by ŕ-chymotrypsin at the three tyrosine residues. The fragments with tyrosine C-terminal residues are candidates of semisynthetic modification. They were isolated and characterized by HPLC, capillary electrophoresis and mass spectrometry.
Semisynthetic preparation of human insulin analogs containing .I.N./I.-methylated B.sup.24./sup.-B.sup.25./sup. or B.sup.25./sup.-B.sup.26./sup. peptide bonds
Klasová, L. ; Huml, Karel ; Barthová, J. ; Ubik, Karel ; Kašička, Václav ; Škarda, Josef ; Hauzerová, Linda ; Barth, Tomislav ; Wollmer, A. ; Brandenburg, D. ; Ježek, Jan ; Velek, Jiří
Desoctapeptideinsulin (DOI), prepared by tryptic cleavage of porcine insulin, was utilized in the enzyme-catalyzed synthesis of human insulin analogs modified in the C-terminal region of the B-chain.
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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