S. Fittkau

Martin Luther University Halle-Wittenberg

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Κ. Peters

Universitäts-Herzzentrum Freiburg-Bad Krozingen

Günther Jahreis

Max Planck Research Unit for Enzymology of Protein Folding

W. Damerau

Max Delbrück Center

Dieter Brömme

University of British Columbia

Heidrun Kirschke

Martin Luther University Halle-Wittenberg

S. Mqotsi

Luther University

Christian Betzel

Universität Hamburg

K.-P. Klante

Luther University

Hans-Dietrich Bergeder

University of Bonn

J.J.L. Mestrom

Freie Universität Berlin

Cooperative Institutions

Martin Luther University Halle-Wittenberg

Luther University

Radboud University Nijmegen

University of Bonn

Centre National de la Recherche Scientifique

Humboldt-Universität zu Berlin

Freie Universität Berlin

All India Institute of Medical Sciences

Bulgarian Academy of Sciences

Hungarian Academy of Sciences

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[Synthesis and properties of 1-chloro-3-amino-4-phenyl-butanone-2, an inhibitor of leucine aminopeptidase from bovine eye lenses].

PubMed (1972)

S. Fittkau

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Citations (1)

Preface

Ophthalmic Research (1979)

Hans Bloemendal Hans-Reinhard Koch Clifford V. Harding Drusilla Harding Stanley Susan

10.1159/000265015

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Vergleichende Untersuchungen über die Ausscheidung von Peptiden im Harn stoffwechselgesunder Personen

Hoppe-Seyler´s Zeitschrift für physiologische Chemie (1961)

S Ansorge S. Fittkau Hugh H. Hanson

Article Vergleichende Untersuchungen über die Ausscheidung von Peptiden im Harn stoffwechselgesunder Personen was published on January 1, 1961 in the journal Biological Chemistry (volume 324, issue Jahresband).

10.1515/bchm2.1961.324.1.17

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Citations (9)

Die Ausscheidung von freiem und peptidgebundenem Aminostickstoff im Harn gesunder Personen unter Einflu\ von 19-Norandrostenolon-phenylpropionat

Zeitschrift für die Gesamte Experimentelle Medizin (1966)

S. Fittkau K.-P. Preusser

Vier gesunden männlichen Versuchspersonen wurden in einmaliger Dosis 50 mg bzw. zweimal 100 mg 19-Norandrostenolonphenylpropionat intramuskulär appliziert und die Ausscheidungsgrö\en an Gesamtstickstoff, Harnstoff-Stickstoff sowie an freiem und peptidgebundenem Aminostickstoff im Harn über 2 Wochen verfolgt. Als Ma\ für einen gesicherten Wirkungseintritt wird die retinierte Stickstoffmenge in Prozent der N-Ausscheidung vor der Medikation ausgedrückt. Die Retentionsquotienten liegen bei Verabfolgung von 50 mg des Anabolikums zwischen 24 und 36%. Nach zweimaliger Injektion von je 100 mg werden ausgeprägte Minima der N-Ausscheidung am 4. und 10. Tag nach Erstapplikation mit Retentionsquotienten von 30 bzw. 52% beobachtet. Der Ausscheidungsverlauf des Harnstoffs folgt dem des Gesamtstickstoffs und liegt konstant zwischen 78 und 84%. Die Elimination an freiem Aminostickstoff wird erst durch Dosen von zweimal 100 mg des Anabolikums beeinflu\t und sinkt in der Hauptperiode im Mittel um 24% gegenüber der Vorperiode ab. Der peptidgebundene Aminostickstoff wird in seiner Ausscheidungsgrö\e durch Nandrolon in keinem der vier Fälle signifikant beeinflu\t. Eine Aufbereitungsmethode des Harns zur Ausschaltung der Amino-säurekonjugate durch Extraktion mit Essigsäureäthylester und spezifischen Erfassung des Peptidstickstoffs wird im Detail mitgeteilt.

10.1007/bf02052195

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Contents, Vol. 11, 1979

Ophthalmic Research (1979)

Hans Bloemendal Hans-Reinhard Koch Clifford V. Harding Drusilla Harding Stanley Susan

10.1159/000265013

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[Thermitase--a thermostable serine protease. VIII. Kinetic and ESR investigations on the interactions of enzymes with spin labeled peptide methyl ketones].

PubMed (1986)

S. Fittkau D Pauli P Bouaravong W. Damerau

An attempt was made to study the structure of the active center of thermitase by means of spin labeled peptide analogues. For this purpose, peptide methyl ketones SL-Alan-PheCH3 of different chain length (n = 0, 1, 2, 3; SL = 2,2,5,5-Tetramethyl-pyrrolin-1-oxyl-3-carbonyl) were synthesized. Synthesis and physico-chemical properties of these compounds are described and inhibition constants Ki for the interaction of these compounds with thermitase were measured. SL-Ala2-PheCH3 and SL-Ala3-PheCH3 are strong reversible inhibitors of thermitase with Ki values of 8.9 X 10(-6) M and 4.8 X 10(-7) M, respectively, whereas the analogous compounds with n = 0 and n = 1 represent only reduced affinity for this enzyme. ESR spectra of SL-Ala2-PheCH3 and SL-Ala3-PheCH3 in the presence of thermitase reveal that a great part of the SL residues of enzyme bound inhibitor molecules is not measurably restricted in their mobility whereas another part is hindered by unspecific interaction with the protein. The kinetic and ESR data are discussed with regard to the substrate binding region of the enzyme.

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Markierte Polypeptide. IV. Synthese von [1‐¹⁴C]Glycin¹⁰‐α‐Melanotropin

Journal für praktische Chemie (1974)

S. Fittkau K. Medzihradszky János Seprődi

Abstract Das melanocytenstimulierende Hormon α‐Melanotropin wurde durch Fragmentkondensation des N‐terminalen Acetyltetrapeptids mit dem Pentapeptid der Sequenz 5 bis 9, Verlängerung des Nonapeptids mit 14 C‐Glycin und Kupplung des radioaktiven Dekapeptids mit dem C‐terminalen Tripeptidamid aufgebaut. Aus dem so erhaltenen geschützten Acetyltridekapeptidamid wurde nach Abspaltung der Schutzgruppen radioaktives α‐Melanotropin mit einer spezifischen Aktivität von 34 mCi/mMol und einer biologischen Aktivität von 2 · 10 10 Einheiten/g erhalten.

10.1002/prac.19743160420

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Potent and selective inactivation of cysteine proteinases with N-peptidyl-O-acyl hydroxylamines

Biochemical Journal (1989)

Dieter Brömme Angelika Schierhorn Heidrun Kirschke Bernd Wiederanders A. Barth

A series of N-peptidyl-O-acyl hydroxylamines was synthesized and tested as inactivators of cysteine proteinases. Depending on the structure of the peptidyl residue of the inhibitors, rapid and complete irreversible inactivation of the lysosomal cathepsins, B, L and S, may be achieved. The most effective inhibitors display second-order rate constants of the inactivation in the range 10(5)-10(6) M-1.s-1. By contrast, the activity of the aminoendopeptidase cathepsin H is only negligibly affected by the N-terminal-protected peptidyl inhibitors.

Cysteine Proteinase Inhibitors

Cathepsin L

Residue (chemistry)

10.1042/bj2630861

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Citations (35)

The Binding Center of Leucine Aminopeptidase

Ophthalmic Research (1979)

S. Fittkau G. Kämmerer W. Damerau

As shown by kinetic experiments with competitive inhibitors like Thr(But)-Phe-X peptide ligands are bound by hydrophobic interactions at two nonpolar subsites S1 and S2. This contact region prefers with high selectivity L-configuration in P1 and P2 position. The additional binding P3-S3 differs in polarity and stereospecifical requirement. The nitroxide-labelled inhibitor Thr(But > Phe-SL is competitively bound at two types of binding sites. The main type, obtained from electron spin resonance spectroscopy, is in agreement with results from kinetic studies and represents the binding of two inhibitor molecules per subunit of the enzyme.

Site-directed spin labeling

10.1159/000265038

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Citations (6)

Amino acid sequence of the tryptic SH‐peptide of thermitase, a thermostable serine proteinase from Thermoactinomyces vulgaris. Relation to the subtilisins

International journal of peptide & protein research (1983)

Miroslav Baudyš V. Kostka Gert Hausdorf S. Fittkau Wolfgang Höhne

The following amino acid sequence of the tryptic SH‐peptide of thermitase, a thermostable serine proteinase from Thermoactinomyces vulgaris , was determined: Val ‐ Val ‐ Gly ‐ Gly ‐ Trp ‐ Asp ‐ Phe ‐ Val‐Asp‐Asn‐Asp‐Ser‐Thr‐Pro‐Gln‐Asn ‐ Gly ‐ Asn ‐ Gly ‐His64‐ Gly ‐ Thr ‐ His ‐Cys68 ‐ Ala‐Gly‐Ile‐Ala‐Ala‐Ala‐Val‐Thr‐Asn ‐ Asn ‐ Ser ‐ Thr ‐ Gly ‐ Ile ‐ Ala ‐ Gly ‐ Thr ‐ Ala ‐ Pro ‐ Lys. This sequence shows homology with the highly conservative part of the subtilisin sequences around the active site His‐64. The single cysteine residue of thermitase is localized near this histidine residue thus replacing valine in position 68 (according to the numbering of the subtilisins). This becomes evident also from the specific labeling of the active site histidine with a radioactive inhibitor (Z‐Ala‐Ala‐Phe‐ 14 CH 2 ‐Cl). The tryptic SH‐peptide isolated from the modified enzyme contains all the radioactivity and has the same end group and amino acid composition as the tryptic peptide isolated from the tryptic digest of the unlabeled enzyme and subjected to sequential analysis. From sequence homology as well as from secondary structure predictions it may be concluded that the geometry of the active site of thermitase is very similar to that of the subtilisins with the cysteine residue nearby. The inactivation of thermitase by labeling of the SH‐group with mercury compounds may then be due to a sterical hindrance or to a more direct interaction of the mercury atom with the charge relay system of the enzyme.

Subtilisin

Serine Proteinase Inhibitors

10.1111/j.1399-3011.1983.tb02069.x

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Citations (18)