-transparent.png){kind=logo}
We have proposed earlier a three gene loci model to explain the expression of the aldo-keto reductases in human tissues. According to this model, aldose reductase is a monomer of alpha subunits, aldehyde reductase I is a dimer of alpha, beta subunits, and aldehyde reductase II is a monomer of delta subunits. Using immunoaffinity methods, we have isolated the subunits of aldehyde reductase I (alpha and beta) and characterized them by immunocompetition studies. It is observed that the two subunits of aldehyde reductase I are weakly held together in the holoenzyme and can be dissociated under high ionic conditions. Aldose reductase (alpha subunits) was generated from human placenta and liver aldehyde reductase I by ammonium sulfate (80% saturation). The kinetic, structural and immunological properties of the generated aldose reductase are similar to the aldose reductase obtained from the human erythrocytes and bovine lens. The main characteristic of the generated enzyme is the requirement of Li2SO4 (0.4 M) for the expression of maximum enzyme activity, and its Km for glucose is less than 50 mM, whereas the parent enzyme, aldehyde reductase I, is completely inhibited by 0.4 M Li2SO4 and its Km for glucose is more than 200 mM. The beta subunits of aldehyde reductase I did not have enzyme activity but cross-reacted with anti-aldehyde reductase I antiserum. The beta subunits hybridized with the alpha subunits of placenta aldehyde reductase I, and aldose reductase purified from human brain and bovine lens. The hybridized enzyme had the characteristic properties of placenta aldehyde reductase I.
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
August 1985,
FEBS letters,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 1985,
Progress in clinical and biological research,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
November 2002,
FEMS microbiology letters,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 2012,
Frontiers in pharmacology,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 2007,
Annual review of pharmacology and toxicology,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 1999,
Advances in experimental medicine and biology,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 1993,
Advances in experimental medicine and biology,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
July 2013,
Toxicology letters,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
January 2010,
Journal of ophthalmology,
S K Srivastava, and
B Das, and
G A Hair, and
R W Gracy, and
S Awasthi, and
N H Ansari, and
J M Petrash
June 2015,
Chemico-biological interactions,
