Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Lawrence M. Pinkus"'
Publikováno v:
European Journal of Pharmacology. 181:283-287
The distribution of 5-HT3 receptor sites was examined in rat brain by autoradiography using 3H-enantiomers of zacopride. The (S)-3H-isomer labelled high densities of binding sites in the hippocampus, amygdala and cortex. The (R)-3H-isomer labelled co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08b429f86a63c67158c61b6fbe2e323f
https://doi.org/10.1016/0014-2999(90)90090-s
https://doi.org/10.1016/0014-2999(90)90090-s
Publikováno v:
European Journal of Pharmacology: Molecular Pharmacology. 188:313-319
A 5-HT3 binding site, with high affinity for (S-)[3H]zacopride, was solubilized from rabbit small bowel muscularis membranes utilizing 0.5% sodium cholate and 400 mM (NH4)2SO4. Approximately 72% of the (S-)[3H]zacopride binding activity was recovered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aff2b7e78670993b6082a7f52841597
https://doi.org/10.1016/0922-4106(90)90191-y
https://doi.org/10.1016/0922-4106(90)90191-y
Publikováno v:
European journal of pharmacology. 192(3)
In ferrets, the oral emetic activity of zacopride was compared with its R- and S-enantiomers. Increasing doses of 0.01, 0.1, 1.0, 10.0 and 31.6 mg/kg of zacopride or its 2 enantiomers were each administered at hourly intervals to separate groups of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad93257f85d12e633838cedb7ff41b9b
https://pubmed.ncbi.nlm.nih.gov/2055236
https://pubmed.ncbi.nlm.nih.gov/2055236
Publikováno v:
European journal of pharmacology. 181(3)
Zacopride administered orally was more emetic in fed than in fasted ferrets. The emetic activity of zacopride (0.1 mg/kg p.o.) was inhibited (100%) by 0.1 mg/kg i.p. of zacopride and 1 mg/kg i.p. of ICS 205–930. Haloperidol (3.16 mg/kg i.p.) and pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27b5c98537108cdf1297f00ae25880a5
https://pubmed.ncbi.nlm.nih.gov/2384137
https://pubmed.ncbi.nlm.nih.gov/2384137
Publikováno v:
European journal of pharmacology. 179(1-2)
[3H]Zacopride exhibits high affinity (Kd less than or equal to 1 nM) for 5-HT3 binding sites (inhibited by ICS 205-930) in rabbit intestinal muscularis and vagus nerve, human jejunum, rat intestinal muscularis and rat brain cortex. Its binding was in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b40c00d8c3300991519e3d856cbc836
https://pubmed.ncbi.nlm.nih.gov/2364986
https://pubmed.ncbi.nlm.nih.gov/2364986
Publikováno v:
Journal of Biological Chemistry. 249:1915-1921
The glutaminase activity of glutamine-dependent carbamyl phosphate synthetase (Escherichia coli) and that of the separated light subunit of this enzyme, as well as the glutaminedependent synthetase activity catalyzed by the native enzyme, are inactiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::71ecf5a53b758acf44fa78a5ad8a7954
https://doi.org/10.1016/s0021-9258(19)42872-x
https://doi.org/10.1016/s0021-9258(19)42872-x
Publikováno v:
Archives of Biochemistry and Biophysics. 234:434-441
Adenylate cyclase from rat kidney membranes solubilized with Lubrol-PX, was resolved into calmodulin-insensitive and calmodulin-sensitive forms using DEAE-Sephacel and calmodulin-Sepharose affinity chromatography. The major fraction, 90% of the activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7347dce796a91406614a9feec10be0d8
https://doi.org/10.1016/0003-9861(84)90290-x
https://doi.org/10.1016/0003-9861(84)90290-x
Publikováno v:
Journal of Biological Chemistry. 249:492-499
The monomer of glutamine-dependent carbamyl phosphate synthetase can be reversibly dissociated to a heavy (mol wt ∼130,000) and a light (mol wt ∼42,000) subunit by treatment with 1 m potassium thiocyanate. The separated heavy subunit can catalyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c2b509a982a09830b137bc85318a8b1
https://doi.org/10.1016/s0021-9258(19)43057-3
https://doi.org/10.1016/s0021-9258(19)43057-3
Autor:
Alton Meister, Lawrence M. Pinkus
Publikováno v:
Journal of Biological Chemistry. 247:6119-6127
Carbamyl phosphate synthetase from Escherichia coli, which is composed of a light and a heavy subunit, is inhibited with respect to its glutamine-dependent reactions by treatment with l-2-amino-4-oxo-5-chloro[5-14C]pentanoic acid. This glutamine anal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a192c0653e6d082484026f0ab9ab3c31
https://doi.org/10.1016/s0021-9258(19)44772-8
https://doi.org/10.1016/s0021-9258(19)44772-8
Publikováno v:
Proceedings of the National Academy of Sciences. 70:2717-2721
Glutamine-dependent carbamylphosphate synthetase ( Escherichia coli ) is composed of a heavy subunit (molecular weight about 130,000) and a light subunit (molecular weight about 42,000), which can be separated with retention of catalytic activities.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a36446c89604623575cfceec68baaae
https://doi.org/10.1073/pnas.70.10.2717
https://doi.org/10.1073/pnas.70.10.2717