Carbonyl reductases were purified from mouse and guinea pig lung. The mouse enzyme exhibited structural and catalytic similarity to the guinea pig enzyme: tetrameric structure consisting of an identical 23 kDa subunit; basicity (pI of 8.8); low substrate specificity for alphatic and aromatic carbonyl compounds; dual cofactor specificity for NADPH and NADH; stereospecific transfer of the 4-pro S hydrogen of NADPH; and sensitivity to pyrazole, 2-mercaptoethanol and ferrous ion. Although 3-ketosteroids were extensively reduced by the mouse enzyme but not by the guinea pig enzyme in the forward reaction, the two enzymes similarly oxidized some alicyclic alcohols such as acenaphthenol, cyclohex-2-en-1-ol and benzenedihydrodiol in the presence of NADP+ and NAD+. A partial similarity between the two enzymes was observed immunologically, using antibodies against the purified guinea pig enzyme. The lung enzymes differ in several aspects from other oxidoreductases from extrapulmonary tissues. The immunoreactive protein was detected only in lung of the tissues of the two species.
All Science Journal Classification (ASJC) codes
- Molecular Biology