Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Karl Peter Rücknagel"'
Autor:
Angelika Schierhorn, Renate Ulbrich-Hofmann, Alexandra Lerchner, Hina Younus, Karl-Peter Rücknagel, Regina Schöps, M. Saleemuddin
Publikováno v:
Journal of Protein Chemistry. 22:499-508
A recombinant phospholipase D from white cabbage (PLD2) composed of 812 amino acid residues was studied by site-directed mutagenesis and limited proteolysis to obtain first information on its tertiary structure. Limited proteolysis by thermolysin res
Publikováno v:
European Journal of Lipid Science and Technology. 104:79-87
Phospholipase D (PLD) from cabbage is interesting as biocatalyst in phospholipid transformation. To provide the basis for genetic engineering of the enzyme, gene cloning and sequencing were carried out. We have recently identified two isoenzymes, PLD
Autor:
Jan R. Andreesen, Karl Peter Rücknagel, Ulf-Martin Kohlstock, Angelika Schierhorn, Michael Reuter, Brigitte Söhling
Publikováno v:
European Journal of Biochemistry. 268:6417-6425
In the amino-acid-fermenting anaerobe Eubacterium acidaminophilum, acetyl phosphate is synthesized by protein C of glycine reductase from a selenoprotein A-bound carboxymethyl-selenoether. We investigated specific thiols present in protein C for resp
Publikováno v:
Biological Chemistry. 382:979-986
A strongly [75]Selabeled 22 kDa protein detected previously showed in its Nterminal sequence the highest similarity to the family of thioldependent peroxidases, now called peroxiredoxins. The respective gene prxU was cloned and analyzed. prxU encodes
Autor:
Andreas Pich, Karl Peter Rücknagel, Ute Kabisch, Andrea Gräntzdörffer, Jan R. Andreesen, Angelika Schierhorn
Publikováno v:
Journal of Biological Chemistry. 274:8445-8454
Highly active d-proline reductase was obtained from Clostridium sticklandiiby a modified purification scheme. The cytoplasmic enzyme had a molecular mass of about 870 kDa and was composed of three subunits with molecular masses of 23, 26, and 45 kDa.
Autor:
Gunter Fischer, Gerlind Stoller, Karl Peter Rücknagel, Jens-U. Rahfeld, Angelika Schierhorn, Thomas Tradler
Publikováno v:
FEBS Letters. 407:184-190
A low degree of amino acid sequence similarity to FK506-binding proteins (FKBPs) has been obtained for the peptidyl prolyl cis/trans isomerase (PPIase) domain of E. coli trigger factor (TF) that was thought to be significant with regard to the enzyma
Publikováno v:
European Journal of Biochemistry. 237:862-869
With the aim to localize the structural region that becomes first accessible to proteolytic attack during thermal unfolding, the proteolysis of ribonuclease A was studied in the temperature range of 20-65 degrees C. Subtilisin, proteinase K, and elas
Publikováno v:
Chembiochem : a European journal of chemical biology. 14(1)
Unique respect: The biological properties of four CsA derivatives were fine-tuned by tractable modifications of the MeBmt residue. The new CsA derivatives share strong inhibitory activity toward cyclophilins (Cyps), but each is unique with respect to
Autor:
Sabine E. Axmann, Axel A. Laminet, Andreas Plückthun, Ernst Jaeger, Karl-Peter Rücknagel, Ralph Zahn
Publikováno v:
Journal of Molecular Biology. 242:150-184
From equilibrium measurements with urea we found a three-state thermodynamic and kinetic folding behavior for the precursor and mature form of Escherichia coli β-lactamase TEM2. The thermodynamic intermediate H of Escherichia coli β-lactamase and i
Autor:
Hans J. Schramm, Ernst Jaeger, Karl-Peter Rücknagel, Wolfgang Schramm, G. J. Arnold, Andreas Billich
Publikováno v:
Biochemical and Biophysical Research Communications. 194:595-600
Previous studies have shown that some peptides derived from one of the terminal amino acid segments of the homodimeric HIV-1 protease show moderate inhibition of this enzyme probably by interfering with the "interface" structure formed by the four te