Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Armin Mehlich"'
Autor:
Roman Hirsch, Karl-Ludwig Kratz, Frank Ballwanz, Armin Mehlich, Thomas A. Ternes, Klaus Haberer
Publikováno v:
Journal of Chromatography A. 815:213-223
For the determination of 18 antibiotics in water samples down to the lower ng/l range, an analytical multi method is presented. The analytes belong to different groups of antibiotics such as penicillins, tetracyclines, sulfonamides and macrolid antib
Publikováno v:
Fresenius' Journal of Analytical Chemistry. 360:498-501
A simple and rapid method is described for the preparation of doubly 13C-labelled benzylpenicillin for use in isotope dilution analyses of benzylpenicillin residues. The product is characterized by IR, NMR, GC/MS and LC/MS. Tissue analyses demonstrat
Publikováno v:
Journal of Protein Chemistry. 8:101-113
The semisynthesis of homologues of aprotinin, the bovine pancreatic trypsin inhibitor, is described. The P1 lysine15 residue was replaced by two methods. The first procedure, which consisted of two enzymatic steps for the incorporation of other amino
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 996:23-29
Aprotinin derivatives with decarboxylated lysine, arginine or valine at position 15, the P1 position of modified aprotinin, were produced semisynthetically. Modified aprotinin with oxidatively deaminated Arg1 and Ala16 was also synthesized. Specific
Publikováno v:
Biochemistry. 26:3544-3551
Gibbs energy, enthalpy, and entropy data were determined for two selectively modified analogues of bovine pancreatic trypsin inhibitor (BPTI) to provide a model free set of thermodynamic parameters that characterize (a) the energetic and entropic con
Autor:
Werner Schröder, Herbert R. Wenzel, Armin Mehlich, Eugen Schnabel, Gerd Reinhardt, Harald Tschesche
Publikováno v:
Biological chemistry Hoppe-Seyler. 369(6)
On incubation of [di-seco-15/16,39/40]aprotinin with human plasmin, porcine pancreatic kallikrein or bovine or porcine trypsin in neutral or slightly alkaline solutions [seco-39/40]aprotinin is slowly formed with enzymatic resynthesis of the reactive
Publikováno v:
Proceedings of the Fifth USSR-FRG Symposium on Chemistry of Peptides and Proteins, Odessa, USSR, May 16–20, 1985
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5051ca570599936040dacb6a35de42c8
https://doi.org/10.1515/9783110858846-014
https://doi.org/10.1515/9783110858846-014
Publikováno v:
European journal of biochemistry. 176(3)
The semisynthesis of homologues of aprotinin (BPTI) is described. The P1 amino acid residue of these homologues was substituted by other amino acids using peptide synthetic methods. The reactive-site-modified inhibitor (with the Lys15-Ala16 peptide b
Autor:
A Feldmann, C F Scott, Jürgen Beckmann, R W Colman, Herbert R. Wenzel, Harald Tschesche, Armin Mehlich
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461595489
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db53b8633ed72a0b187e64178f598b7d
https://pub.uni-bielefeld.de/record/1948401
https://pub.uni-bielefeld.de/record/1948401