National Repository of Grey Literature 28 records found  previous11 - 20next  jump to record: Search took 0.00 seconds. 
New means for the induction of ovulation in fish
Barth, Tomislav ; Barthová, J. ; Hamáčková, J. ; Kouřil, J.
Alist of newly found natural GnRH peptides is given. New drugs composed of synthetic GnRH analogues and some dopaminergic inhibitors (Dagin, Ovopel, Aquaspawn) are presented as means for the artificial propagation of fish.
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.
New potential precursors of small biologically active peptides
Straková, Jana ; Klasová, Lenka ; Barthová, J. ; Barth, Tomislav
Five precursors of small biologically active peptides were prepared by enzymatic semisynthesis. Two naturally occurring enkephalins and three enkephalin analogs were attached to desoctapeptide insulin.
Fluorescent labeled amino acid utilizable in solid phase peptide synthesis
Ciencialová, Alice ; Klasová, Lenka ; Jiráček, Jiří ; Barthová, J. ; Barth, Tomislav
Synthesis of fluorescent derivatives of lysine fluorescent probes: 4-phenylspiro[furan-2(3.I.H./I.),1'-phthalan]-3,3'-dione (fluorescamine) and 4-chloro-7-nitrobenzo[1,2,5]oxadiazole (NBD-Cl) utilizable in solid phase peptide synthesis is presented.
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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