Zobrazeno 1 - 10
of 45
pro vyhledávání: '"A. S. Duhaiman"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1597:67-73
o-Phthalaldehyde, a bifunctional cross-linking reagent, is commonly used as a probe for the active site of enzymes. In this study, the interaction of o-phthalaldehyde with camel lens zeta-crystallin was examined by activity and fluorescence measureme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30710fa6af1a904bdfa618b358429646
https://doi.org/10.1016/s0167-4838(02)00272-8
https://doi.org/10.1016/s0167-4838(02)00272-8
Autor:
Nayyar Rabbani, Ali S. Duhaiman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1388:175-180
Camel lens zeta-crystallin was inhibited by pyridoxal-5'-phosphate (PAL-P) and o-phthalaldehyde. PAL-P inactivated zeta-crystallin in a time- and concentration-dependent manner. The initial rate of inactivation followed pseudo-first-order kinetics wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56a9eef6c286cba1f5d5339f30c0465a
https://doi.org/10.1016/s0167-4838(98)00185-x
https://doi.org/10.1016/s0167-4838(98)00185-x
Publikováno v:
Journal of Enzyme Inhibition. 13:229-236
Chlorophenols comprise a major class of environmental contaminants. They are extensively used as insecticides, fungicides, mold inhibitors, antiseptics and disinfectants. We found some of these compounds to be strong inhibitors of zeta-crystallin. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fea513fecc495de8ee14d7acc0efa0d7
https://doi.org/10.3109/14756369809028343
https://doi.org/10.3109/14756369809028343
Publikováno v:
IUBMB Life. 41:415-421
Camel lens zeta-crystallin/NADPH:quinone oxidoreductase activity was inhibited by chloranilic acid (2,5-dichloro-3,6-dihydroxy-1,4-benzoquinone) with NADPH as an electron donor and 9,10-phenanthrenequinone (PQ) as an electron acceptor in a time-indep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d7c8017160d74ed3611ea781c1abbcf
https://doi.org/10.1080/15216549700201431
https://doi.org/10.1080/15216549700201431
Autor:
Ali S. Duhaiman
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 28:1163-1168
Camel lens zeta-crystallin is an NADPH:quinone oxidoreductase, showing limited quinone substrate specificity: among the quinones tested, the orthoquinones were the best substrates. The kinetic mechanism of NADPH:quinone oxidoreductase activity of zet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f59fe6cb25399aa94595a6afe85a1ec8
https://doi.org/10.1016/1357-2725(96)00048-9
https://doi.org/10.1016/1357-2725(96)00048-9
Autor:
Ali S. Duhaiman
Publikováno v:
Journal of Protein Chemistry. 15:261-264
A structure-activity study was carried out to determine the important groups of coumarin derivatives in inhibiting the oxidoreductase activity of the camel lens zeta-crystallin. Coumarin, 4-hydroxycoumarin, 7-hydroxy-4-methylcoumarin, dicoumarol, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9704239b4da40866ca56784431a2fbd8
https://doi.org/10.1007/bf01887114
https://doi.org/10.1007/bf01887114
Autor:
Abdulaziz A. Al-Jafari, Nayyar Rabbani, Abdullah S. Alhomida, Ali S. Duhaiman, Mohammad Amjad Kamal
Publikováno v:
Biochimie. 78:46-50
Acetylcholinesterase (AChE) has been identified and purified from the venom of desert cobra (W aegyptia) to apparent homogeneity using a TSK G 3000 SW gel filtration column and a Mono Q anion-exchange column. AChE was purified to homogeneity as estab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::796bae3757ef7c2fdd6b542dbab07acc
https://doi.org/10.1016/0300-9084(96)81328-9
https://doi.org/10.1016/0300-9084(96)81328-9
Publikováno v:
Biochemical and Biophysical Research Communications. 215:632-640
zeta-crystallin a novel NADPH: quinone oxidoreductase was purified from the cortex of the camel (Camelus dromedarius) lens to homogeneity by Sepharose CL-6B gel filtration column and 2', 5' ADP-Sepharose 4B affinity column chromatography in the prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfae57e1df5fbdb1edca18f00adecacb
https://doi.org/10.1006/bbrc.1995.2511
https://doi.org/10.1006/bbrc.1995.2511
Publikováno v:
Molecular and Cellular Biochemistry. 151:21-26
Acetylcholinesterase (AChE) was investigated in Walterinnesia aegyptia venom and characterized with respect to its kinetic properties. It was found that 4.0 micrograms of crude venom protein and an incubation time of 4.0 min were suitable conditions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bfb829971c6b86f581425ab4f9cdf62
https://doi.org/10.1007/bf01076891
https://doi.org/10.1007/bf01076891
The Mode of Inhibition of Human Erythrocyte Membrane-Bound Acetylcholinesterase by Cisplatinin Vitro
Publikováno v:
Journal of Enzyme Inhibition. 8:281-289
The effect of the well known anticancer drug “cisplatin” on the human erythrocyte membrane-bound acetylcholinesterase (AChE) has been investigated. It was found that cisplatin has inhibitory activity against AChE. Cisplatin (0.5-7.0 mM) inhibited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94de4cca93467e607776d3bc8b066fec
https://doi.org/10.3109/14756369509020135
https://doi.org/10.3109/14756369509020135