Results 151 to 160 of about 30,602 (201)
Some of the next articles are maybe not open access.
Biochemical Pharmacology, 1977
Abstract Rat liver aldehyde reductase is a soluble constitutive enzyme having the ability to catalyze the reduction of several natural aldehydes such as lactaldehyde, glyceraldehyde, glyceraldehyde-3-phosphate, glucuronate, glucuronolactone, and succinic semialdehyde.
R L, Felsted, D R, Richter, N R, Bachur
openaire +2 more sources
Abstract Rat liver aldehyde reductase is a soluble constitutive enzyme having the ability to catalyze the reduction of several natural aldehydes such as lactaldehyde, glyceraldehyde, glyceraldehyde-3-phosphate, glucuronate, glucuronolactone, and succinic semialdehyde.
R L, Felsted, D R, Richter, N R, Bachur
openaire +2 more sources
Inhibition of aldehyde reductase by aldose reductase inhibitors
Biochemical Pharmacology, 1990A broad group of structurally diverse aldose reductase inhibitors including flavonoids, carboxylic acids and hydantoins, have been examined for their ability to inhibit rat kidney aldehyde reductase (EC 1.1.1.19, EC 1.1.1.20) versus rat lens aldose reductase (EC 1.1.1.21).
S, Sato, P F, Kador
openaire +2 more sources
Journal of Neurochemistry, 1985
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
openaire +2 more sources
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
openaire +2 more sources
Structure and Mechanism of Aldehyde Reductase
1995Aldehyde reductase (ALR1, EC 1.1.1.2) and aldose reductase (ALR2, EC 1.1.1.21) catalyze the NADPH-dependent reduction of a wide range of aromatic and aliphatic aldehydes to their corresponding alcohols. Despite a recently expressed opinion that aldose reductase is of little consequence (Harding, 1992) the past few years have seen a great advancement in
T G, Flynn +3 more
openaire +2 more sources
Human kidney aldose and aldehyde reductases
Journal of Diabetes and its Complications, 1993Mounting experimental evidence links increased aldose reductase activity with diabetes-related kidney functional changes. To investigate the interrelationship of NADPH-dependent reductases in the human kidney, both aldose reductase and aldehyde reductase were purified from human kidney by a series of chromatographic procedures, including gel filtration
S, Sato, P F, Kador
openaire +2 more sources
Structure of porcine aldehyde reductase holoenzyme
Nature Structural Biology, 1995Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by x-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 A resolution ...
O, el-Kabbani +5 more
openaire +2 more sources
1980
Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Aves indicating ...
W S, Davidson, T G, Flynn
openaire +2 more sources
Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Aves indicating ...
W S, Davidson, T G, Flynn
openaire +2 more sources
Aldose and aldehyde reductases in human tissues
Biochimica et Biophysica Acta (BBA) - General Subjects, 1984Immunochemical characterizations of aldose reductase and aldehyde reductases I and II, partially purified by DEAE-cellulose (DE-52) column chromatography from human tissues, were carried out by immunotitration, using antisera raised against the homogenous preparations of human and bovine lens aldose reductase and human placenta aldehyde reductase I and
S K, Srivastava +3 more
openaire +2 more sources
Stereospecificity of hydrogen transfer of aldehyde reductase
Experientia, 1979Aldehyde reductase from human liver catalyzes the hydrogen transfer from the pro-4R position on the dihydronicotinamide ring of the coenzyme to the re face of the carbonyl carbon atom of the substrate.
B, Wermuth +2 more
openaire +2 more sources
Multiple Aldehyde Reductases of Human Brain
1980Human brain contains four forms of aldehyde reducing enzymes. One major activity, designated AR3, has properties indicating its identity with the NADPH-dependent aldehyde reductase, EC 1.1.1.2. The other major form of human brain enzyme, AR1, which is also NADPH-dependent, reduces both aldehyde and ketone-containing substrates, including vitamin K3 ...
P L, Hoffman +2 more
openaire +2 more sources

