Tags

Type your tag names separated by a space and hit enter

Characterization of pulmonary carbonyl reductase of mouse and guinea pig.
Biochim Biophys Acta. 1986 Jun 19; 882(2):220-7.BB

Abstract

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 aliphatic 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.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3085728

Citation

Nakayama, T, et al. "Characterization of Pulmonary Carbonyl Reductase of Mouse and Guinea Pig." Biochimica Et Biophysica Acta, vol. 882, no. 2, 1986, pp. 220-7.
Nakayama T, Yashiro K, Inoue Y, et al. Characterization of pulmonary carbonyl reductase of mouse and guinea pig. Biochim Biophys Acta. 1986;882(2):220-7.
Nakayama, T., Yashiro, K., Inoue, Y., Matsuura, K., Ichikawa, H., Hara, A., & Sawada, H. (1986). Characterization of pulmonary carbonyl reductase of mouse and guinea pig. Biochimica Et Biophysica Acta, 882(2), 220-7.
Nakayama T, et al. Characterization of Pulmonary Carbonyl Reductase of Mouse and Guinea Pig. Biochim Biophys Acta. 1986 Jun 19;882(2):220-7. PubMed PMID: 3085728.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of pulmonary carbonyl reductase of mouse and guinea pig. AU - Nakayama,T, AU - Yashiro,K, AU - Inoue,Y, AU - Matsuura,K, AU - Ichikawa,H, AU - Hara,A, AU - Sawada,H, PY - 1986/6/19/pubmed PY - 1986/6/19/medline PY - 1986/6/19/entrez SP - 220 EP - 7 JF - Biochimica et biophysica acta JO - Biochim. Biophys. Acta VL - 882 IS - 2 N2 - 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 aliphatic 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. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/3085728/Characterization_of_pulmonary_carbonyl_reductase_of_mouse_and_guinea_pig_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0304-4165(86)90158-3 DB - PRIME DP - Unbound Medicine ER -