National Repository of Grey Literature 62 records found  beginprevious31 - 40nextend  jump to record: Search took 0.01 seconds. 
CAMM of vasopressin analogs
Huml, Karel ; Barth, Tomislav
Vasopressin and its nonapeptide analogs were studied using computer aided molecular modeling (CAMM) methods to elucidate their structure-bioactivity relationships. The results are discussed in relation to experimentally obtained data of these peptides concerning their biological activities.
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.
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.

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