Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Hans-Gerhard Löffler"'
Autor:
Jark Böttcher, Hans-Gerhard Löffler, Andrej Hasilik, Gerhard Klebe, Torsten Luksch, Christoph A. Sotriffer, Jörg Rademann, Steffen Weik, Andreas Evers
Publikováno v:
ChemMedChem. 1:445-457
A synthetic concept is presented that allows the construction of peptide isostere libraries through polymer-supported C-acylation reactions. A phosphorane linker reagent is used as a carbanion equivalent; by employing MSNT as a coupling reagent, the
Autor:
Stephan Storch, Thomas Braulke, Andrej Hasilik, Hans-Gerhard Löffler, Sanna Partanen, Jaana Tyynelä
The substitution of an active-site aspartic acid residue by asparagine in the lysosomal protease cathepsin D (CTSD) results in a loss of enzyme activity and severe cerebrocortical atrophy in a novel form of neuronal ceroid lipofuscinosis in sheep [Ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f26e85f8cf593645e65b5fb484aa6b00
https://europepmc.org/articles/PMC1223066/
https://europepmc.org/articles/PMC1223066/
Publikováno v:
Zeitschrift für Naturforschung C. 36:751-754
Dedicated to Prof. H. Zahn on the Ocassion of His 65th Birthday Zn+2/Co+2 Exchange, Microbial Acylamino Acid Amido Hydrolase, Aspergillus oryzae, Kinetic Properties The inactivation of the Zn+2 metallo enzyme acylamino acid amido hydrolase from Asper
Publikováno v:
Biological Chemistry Hoppe-Seyler. 369:559-566
We present data indicating that aminoacylase I (EC 3.5.1.14) from porcine kidney and 'renal dipeptidase' (EC 3.4.13.11) are closely related. We show that, in situ, a considerable fraction of aminoacylase activity ist attached to membranes. Incubation
Publikováno v:
Zeitschrift für Naturforschung B. 26:43-46
The pH-dependence of the second order rate constants of the reaction of papain with bromoacetamide in the pH-range 5,5-8,5 is described by a curve with a turning point corresponding to a pK 7,3 ± 0,1 at 25°. This is the pK of a catalytically essent
Publikováno v:
Zeitschrift fur Naturforschung. Section C, Biosciences. 36(11-12)
The kinetics of inactivation of the Zn2+-metalloenzyme acyl-amino acid amido hydrolase by chelating ligands were studied. The rate of inactivation by 1,10-phenanthroline is enhanced by histidine and inhibited in the presence of phenyl-alanine. Remova
Publikováno v:
FEBS letters. 49(2)
Autor:
K.-H. Röhm, Hans-Gerhard Löffler
Publikováno v:
Zeitschrift fur Naturforschung. Section C, Biosciences. (5-6)
Yeast Aminopeptidase I, Molecular Forms, Immunological Behaviour Yeast aminopeptidase I, when purified from autolysates of brewer’s yeast, is obtained in two molecular forms a) the enzymatically active dodecameric complex (Mr = 640 000, s20, w = 22
Publikováno v:
Biological chemistry Hoppe-Seyler. 368(5)
Aminoacylase is inactivated by 2-ethoxy-1-(ethoxycarbonyl)-1,2-dihydroquinoline (EEDQ), a specific carboxyl reagent; inactivation is pH-dependent. The inhibition kinetics were of the first-order type. pH titration shows that half-maximal inactivation