Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Mosé Da Prada"'
Autor:
Cesura Andrea, Mosé Da Prada, Urs Röthlisberger, Hans-Werner Lahm, Rene Imhof, J. Gottowik, Gabrielle Lang, Pari Malherbe
Publikováno v:
European Journal of Biochemistry. 236:996-1002
The structural features of the active site of human monoamine oxidase B (MAO-B) were investigated by affinity labeling and site-directed mutagenesis. The pseudosubstrate inhibitor N-[2-aminoethyl]-5-chloro-2-pyridine carboxamide HCl (lazabemide) can
Publikováno v:
European Journal of Biochemistry. 230:934-942
Monoamine oxidases (MAO) A and B show a high degree of amino acid similarity. Apart from the NH2-terminus, which contains an ADP-binding consensus sequence, little is known about their structural features or the sequences involved in the binding of s
Publikováno v:
European Journal of Pharmacology. 273:215-221
In vivo brain microdialysis was used to assess the effects of tolcapone, a novel central and peripheral inhibitor of catechol-O-methyltransferase on striatal 3,4-dihydroxyphenyl-L-alanine (L-dopa) and dopamine metabolism. The oral administration of 3
Autor:
Mosé Da Prada, Patrick Caspers, Hans-Werner Lahm, Cesura Andrea, Francis Vilbois, Gabrielle Lang, Catherine Karrer
Publikováno v:
European Journal of Biochemistry. 222:377-386
Technological advances in the field of mass spectrometry (MS) are providing powerful analytical means for the investigation of proteins and peptides. In the present work we have used pneumatically assisted electrospray (ion-spray) MS for the biochemi
Publikováno v:
European Journal of Biochemistry. 194:825-829
Synaptophysin, an integral membrane protein of synaptic vesicles in nerve terminals and a class of small translucent vesicles in neuroendocrine cells, was detected in intact rabbit platelets by immunoblotting, immunofluorescence staining and immuno-e
Publikováno v:
Biochemical Pharmacology. 39:216-220
In the present paper we describe the use of digitonin as a suitable detergent for the effective solubilization of MAO-B from human platelets and frontal cortex membrane preparations and the characteristics of the solubilized enzyme using the selectiv
Publikováno v:
Biomedical chromatography : BMC. 10(1)
A non-radiometric method to measure the catechol-O-methyltransferase (COMT) activity in erythrocytes was modified to increase its sensitivity four-fold as well as its reproducibility and applicability. The method is based on the COMT-mediated O-methy
Publikováno v:
FEBS letters. 317(1-2)
Monoamine oxidase (MAO)-A and MAO-B are FAD-containing mitochondrial enzymes which catabolize biogenic and xenobiotic amines. The N-terminal regions of both forms of MAO contain an ADP-binding consensus sequence found in several dinucleotide-dependen
Autor:
Giuseppe Virgallita, V. Miggiano, Hans-Werner Lahm, Barbara Bertocci, Gerhard Zürcher, Gianni Garotta, Mosé Da Prada
Publikováno v:
Biochimica et biophysica acta. 1080(2)
Monoclonal antibodies (mAbs) against the soluble form (S-COMT) of catechol-O-methyltransferase (COMT, EC 2.1.1.6) were produced using a purified preparation of the enzyme from pig liver as antigen. The selected monoclonal antibodies recognized the en
Publikováno v:
Helvetica Chimica Acta. 72:952-968
3-Nitro- and 3-cyanopyrocatechols bearing electron-withdrawing substituents at C(5) have been found to inhibit the enzyme catechol-O-methyltransferase. Structure-activity studies are discussed on the basis of the pharmocological data of 50 compounds