Národní úložiště šedé literatury Nalezeno 6 záznamů.  Hledání trvalo 0.01 vteřin. 
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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