Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by SAWADA, H.
Right arrow Articles by KATO, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by SAWADA, H.
Right arrow Articles by KATO, F.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1980, Vol. 87, No. 4 1153-1165
© 1980 Japanese Biochemical Society

research-article

Reductases for Aromatic Aldehydes and Ketones from Rabbit Liver

Purification and Characterization

Hideo SAWADA, Akira HARA, Toshihiro NAKAYAMA and Fumiko KATO

Department of Biochemistry, Gifu College of Pharmacy Mitahora-higashi, Gifu, Gifu 502

Four aldehyde reductases, F1, F2, F3, and F4, were isolated from rabbit liver cytosol to homogeneity by various chromatographic techniques. F2 is an aldehyde reductase with a molecular weight of 32,000, which resembled aldehyde reductases of human liver and pig kidney in properties. It was inhibited in a noncompetitive way by {alpha}-ketoglutarate and oxaloacetate with K1 values of 4×10––5m. The other three enzymes were NADPH-dependent aromatic aldehyde-ketone reductases. F1 and F3 were monomeric enzymes with molecular weights of 38,000 and 29,000, respectively. F4 showed a molecular weight of 78,000 on gel filtration, but sodium dodecyl sulfate gel electrophoresis revealed two different subunits with molecular weights of 26,000 and 24,000. The molar ratio of NADPH: F1, F2, or F3 binding was 1 : 1, whereas that of NADPH: F4 binding was 3 : 1. The number of thiol groups in one molecule of F1, F2, F3, and F4, was 4, 4, 4, and 5, respectively. The enzyme activity of F3 was inhibited by addition of an equal mole amount of PCMB. Only F4 was inhibited by metal chelating agents.

F1 also catalyzed the interconversion of 3(17)-keto and 3(17)ß-hydroxysteroids, whereas F3 catalyzed oxidoreduction of some 3{alpha}-hydroxysteroids of the 5{alpha}-series. These results suggest that F1 and F3 are 3(17)ß-hydroxysteroid dehydrogenase and 3{alpha}-hydroxysteroid dehydrogenase, respectively. Endogenous substrates for F4 could not be identified in this work. F1 showed the lowest Km value for reduction of aldehydes and ketones among the four reductases. It has been suggested that F1 is the primary enzyme responsible for the reduction of endogenous aldehydes and xenobiotic aldehydes and ketones in vivo.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Biol. Reprod.Home page
C. Gaudreault, C. Légaré, B. Bérubé, and R. Sullivan
Hamster Sperm Protein, P26h: A Member of the Short-Chain Dehydrogenase/Reductase Superfamily
Biol Reprod, July 1, 1999; 61(1): 264 - 273.
[Abstract] [Full Text]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.