Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Regina Pietruszko"'
Publikováno v:
Scopus-Elsevier
K(m) and V(max) values for 10 coenzyme analogs never previously studied with any aldehyde dehydrogenase and NADP(+) were compared with those for NAD(+) for three human aldehyde dehydrogenases (EC 1.2.1.3); the cytoplasmic E1 (the product of the aldh1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f5f7e0aa6d53e1206f93cc776d82a7d
https://doi.org/10.1080/07391102.2001.10506752
https://doi.org/10.1080/07391102.2001.10506752
Publikováno v:
Chemico-Biological Interactions. :103-114
4-trans-(N,N-dimethylamino)cinnamaldehyde (DACA) is a chromophoric and fluorogenic substrate of aldehyde dehydrogenase. Fluorescence of DACA is enhanced by binding to aldehyde dehydrogenase in the absence of catalysis both in the presence and absence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6aca18a1162f6b01d9e448b2c369d30
https://doi.org/10.1016/s0009-2797(00)00226-x
https://doi.org/10.1016/s0009-2797(00)00226-x
Publikováno v:
Journal of Biological Chemistry. 274:33366-33373
Purification and characterization of enzymes metabolizing retinaldehyde, propionaldehyde, and octanaldehyde from four human livers and three kidneys were done to identify enzymes metabolizing retinaldehyde and their relationship to enzymes metabolizi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fc7af2b02e80408cf83102afaf86788
https://doi.org/10.1074/jbc.274.47.33366
https://doi.org/10.1074/jbc.274.47.33366
Publikováno v:
European Journal of Biochemistry. 262:704-712
Low concentrations of citral (3,7-dimethyl-2,6-octadienal), an inhibitor of retinoic acid biosynthesis, inhibited E1, E2 and E3 isozymes of human aldehyde dehydrogenase (EC1.2.1.3). The inhibition was reversible on dilution and upon long incubation i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76b59427c6b4b6ba61674f16c3b301d0
https://doi.org/10.1046/j.1432-1327.1999.00415.x
https://doi.org/10.1046/j.1432-1327.1999.00415.x
Autor:
Ming-Kai Chern, Regina Pietruszko
Publikováno v:
Biochemical and Biophysical Research Communications. 213:561-568
The E3 isozyme of human aldehyde dehydrogenase (EC 1.2.1.3), with broad substrate specificity, which also catalyzes dehydrogenation of 4-aminobutyraldehyde, was purified and sequenced recently (1,3). It has been shown during this investigation to hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8af8c4cb178968cf65d43da5e59270b
https://doi.org/10.1006/bbrc.1995.2168
https://doi.org/10.1006/bbrc.1995.2168
Autor:
N. Mukerjee, Regina Pietruszko
Publikováno v:
Journal of Biological Chemistry. 269:21664-21669
Isosorbide dinitrate inactivated E1 and E2 isozymes of human aldehyde dehydrogenase (EC 1.2.1.3), abolishing both dehydrogenase and esterase activities. NAD promoted, whereas chloral and NAD protected the enzyme from inactivation. The inactivation wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e78346d10cbe0a14d66f8856a7417240
https://doi.org/10.1016/s0021-9258(17)31857-4
https://doi.org/10.1016/s0021-9258(17)31857-4
Publikováno v:
Biochemical Journal. 282:353-360
4-trans-(NN-Dimethylamino)cinnamaldehyde (an aldehyde, DACA) and 4-trans-(NN-dimethylamino)cinnamoylimidazole (an amide, DACI) have been shown to be substrates for human aldehyde dehydrogenase (EC 1.2.1.3) which form chromophoric covalent intermediat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::875dddb2a27b5ccefc5f7139a76fb0a6
https://doi.org/10.1042/bj2820353
https://doi.org/10.1042/bj2820353
Publikováno v:
Alcohol. 8:25-30
Aldehyde dehydrogenase (EC 1.2.1.3) has been purified to homogeneity from Sprague-Dawley rat liver mitochondrial matrix; its specific activity with propionaldehyde (1 mM at pH 9.0) is 1.4 mumol/min/mg. It has a native molecular weight of ca. 260,000
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::883bc4abff418971a21da0e831517ffa
https://doi.org/10.1016/0741-8329(91)91184-4
https://doi.org/10.1016/0741-8329(91)91184-4
Publikováno v:
Biochemical Journal. 266:179-187
Bromoacetophenone (2-bromo-1-phenylethanone) has been characterized as an affinity reagent for human aldehyde dehydrogenase (EC 1.2.1.3) [MacKerell, MacWright & Pietruszko (1986) Biochemistry 25, 5182-5189], and has been shown to react specifically w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c5f66995ddf7be4def4a30eb359519d
https://doi.org/10.1042/bj2660179
https://doi.org/10.1042/bj2660179
Autor:
Darryl P. Abriola, Regina Pietruszko
Publikováno v:
Encyclopedia Of Molecular Medicine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a8822fc8ab2777f382f33c17c3b0ba0a
https://doi.org/10.1002/0471203076.emm0378
https://doi.org/10.1002/0471203076.emm0378
