Interrelationships among human aldo-keto reductases: Immunochemical, kinetic and structural properties

Satish Srivastava, Ballabh Das, Gregory A. Hair, Robert W. Gracy, Sanjay Awasthi, Naseem Ansari, J. Mark Petrash

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Abstract

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 α subunits, aldehyde reductase I is a dimer of α, β subunits, and aldehyde reductase II is a monomer of δ subunits. Using immunoaffinity methods, we have isolated the subunits of aldehyde reductase I (α and β) 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 (α 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 K(m) for glucose is less than 50 mM, whereas the parent enzyme, aldehyde reductase I, is completely inhibited by 0.4 M Li2SO4 and its K(m) for glucose is more than 200 mM. The β subunits of aldehyde reductase I did not have enzyme activity but cross-reacted with anti-aldehyde reductase I antiserum. The β subunits hybridized with the α 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.

Original languageEnglish (US)
Pages (from-to)334-343
Number of pages10
JournalBiochimica et Biophysica Acta - General Subjects
Volume840
Issue number3
DOIs
StatePublished - 1985

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Aldehyde Reductase
Structural properties
Kinetics
Placenta
Enzymes
Enzyme activity
L-glucuronate reductase
carbonyl reductase (NADPH)
Lenses
Monomers
Glucose
Holoenzymes
Ammonium Sulfate
Dimers
Liver

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Interrelationships among human aldo-keto reductases : Immunochemical, kinetic and structural properties. / Srivastava, Satish; Das, Ballabh; Hair, Gregory A.; Gracy, Robert W.; Awasthi, Sanjay; Ansari, Naseem; Petrash, J. Mark.

In: Biochimica et Biophysica Acta - General Subjects, Vol. 840, No. 3, 1985, p. 334-343.

Research output: Contribution to journalArticle

Srivastava, Satish ; Das, Ballabh ; Hair, Gregory A. ; Gracy, Robert W. ; Awasthi, Sanjay ; Ansari, Naseem ; Petrash, J. Mark. / Interrelationships among human aldo-keto reductases : Immunochemical, kinetic and structural properties. In: Biochimica et Biophysica Acta - General Subjects. 1985 ; Vol. 840, No. 3. pp. 334-343.
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