Document Detail


Purification and characterization of aldo-keto reductases from gerbil liver: immunochemical evidence for related proteins in other mammalian species.
MedLine Citation:
PMID:  3541787     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We purified a hepatic aldehyde reductase (AR1) and two carbonyl reductases (CR1, CR2) from the Mongolian gerbil, an animal recently shown to closely resemble man in its metabolism of a carbonyl containing organochlorine pesticide. The apparent molecular weights of AR1, CR1, and CR2 were 40,700, 33,000, and 34,700, respectively. Typical of similar enzymes in other species, gerbil AR1 reduced aliphatic and aromatic aldehydes and was inhibited by phenobarbital or valproate, whereas CR1 and CR2 catalyzed the reduction of aromatic aldehydes and ketones as well as quinones and were inhibited by p-chloromercuribenzoate, mercuric chloride, or pyrazole. All three enzymes were insensitive to metal chelating agents and utilized NADPH as their cofactor. CR1 was unique in being equally active with NADH as its cofactor. Antibodies raised against CR1 reacted with purified CR1 and CR2, but not with AR1, as judged by immunoblot analyses. There were three immunochemically related proteins in gerbil liver cytosol (30 to 35 kDa range) recognized by the anti-CR1 IgG. Similar immunoblot analyses of hepatic cytosolic proteins from other mammalian species revealed immunoreactive proteins only in the hamster, the rabbit, and man, and not in the rat, the mouse, or the guinea pig. Quantitative immunoblot analyses of human liver cytosol from seven patients revealed three immunoreactive proteins. These were present in unequal and varying concentrations, although there were only small interindividual differences in the total concentration of the immunoreactive proteins. We conclude that there are multiple molecular forms of immunochemically related hepatic carbonyl reductases in the gerbil and in some other mammalian species, including man.
Authors:
D T Molowa; S A Wrighton; P S Guzelian
Related Documents :
3792387 - Carbamyl phosphate synthetase i deficiency with no detectable mrna activity.
2541017 - The primary structure of rat ribosomal protein l18a.
8136027 - Purification and partial sequence of proteins involved in the cholic acid transport int...
1893527 - Production of antibodies to peptide sequences present in human o6-alkylguanine-dna alky...
10489357 - Characterization of human herpesvirus-8 k8.1a/b glycoproteins by monoclonal antibodies.
14712277 - Vernalization requires epigenetic silencing of flc by histone methylation.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  251     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1986 Dec 
Date Detail:
Created Date:  1987-02-05     Completed Date:  1987-02-05     Revised Date:  2014-03-18    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  487-94     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Alcohol Oxidoreductases / genetics,  isolation & purification*,  metabolism
Animals
Chromatography, DEAE-Cellulose
Cricetinae
Cytosol / enzymology
Electrophoresis, Polyacrylamide Gel
Gerbillinae / metabolism*
Guinea Pigs
Immunochemistry
Liver / enzymology*
Mesocricetus
Mice
Rabbits
Rats
Rats, Inbred Strains
Species Specificity
Grant Support
ID/Acronym/Agency:
ES-01519/ES/NIEHS NIH HHS; ES-07087/ES/NIEHS NIH HHS
Chemical
Reg. No./Substance:
EC 1.1.-/Alcohol Oxidoreductases; EC 1.1.1.21/carbonyl reductase (NADPH)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Polyamine binding sites on Escherichia coli ribosomes.
Next Document:  Characterization of an enzyme that is capable of processing pro-gonadotropin-releasing hormone prote...