Tags

Type your tag names separated by a space and hit enter

Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver.
Biochem J. 1984 Nov 01; 223(3):697-705.BJ

Abstract

Two forms of microsomal carbonyl reductase, solubilized in Triton X-100, were purified to homogeneity from the liver of male guinea pigs, primarily by affinity, DEAE-Sephacel, gel-filtration and hydroxyapatite chromatography. The major form was a tetrameric glycoprotein of single subunits of Mr 32000 and a pI value of 7.0; another minor form was a monomeric protein with Mr 34000 and a pI value of 7.8. The enzymes were immunologically distinct. Although the enzymes showed similar substrate specificity for exogenous aldehydes and ketones and apparently absolute cofactor specificity for NADPH, their specificity for natural carbonyl compounds differed. The major form irreversibly reduced 5 alpha- and 5 beta-dihydrotestosterones, menadione and lauryl aldehyde with low Km values of 10-70 microM, whereas the minor form not only reduced 17-oxosteroids, of which 3 alpha-hydroxy-5 beta-androstan-17-one was the best substrate, but also oxidized 17-hydroxysteroids in the presence of NADP+. The two forms of carbonyl reductase also exhibited different sensitivity to heavy metal ions, dicoumarol, tetramethyleneglutaric acid, phenobarbitone and corticosteroids.

Authors

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

Pub Type(s)

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

Language

eng

PubMed ID

6439186

Citation

Usui, S, et al. "Purification and Characterization of Two Forms of Microsomal Carbonyl Reductase in Guinea Pig Liver." The Biochemical Journal, vol. 223, no. 3, 1984, pp. 697-705.
Usui S, Hara A, Nakayama T, et al. Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver. Biochem J. 1984;223(3):697-705.
Usui, S., Hara, A., Nakayama, T., & Sawada, H. (1984). Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver. The Biochemical Journal, 223(3), 697-705.
Usui S, et al. Purification and Characterization of Two Forms of Microsomal Carbonyl Reductase in Guinea Pig Liver. Biochem J. 1984 Nov 1;223(3):697-705. PubMed PMID: 6439186.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver. AU - Usui,S, AU - Hara,A, AU - Nakayama,T, AU - Sawada,H, PY - 1984/11/1/pubmed PY - 1984/11/1/medline PY - 1984/11/1/entrez SP - 697 EP - 705 JF - The Biochemical journal JO - Biochem. J. VL - 223 IS - 3 N2 - Two forms of microsomal carbonyl reductase, solubilized in Triton X-100, were purified to homogeneity from the liver of male guinea pigs, primarily by affinity, DEAE-Sephacel, gel-filtration and hydroxyapatite chromatography. The major form was a tetrameric glycoprotein of single subunits of Mr 32000 and a pI value of 7.0; another minor form was a monomeric protein with Mr 34000 and a pI value of 7.8. The enzymes were immunologically distinct. Although the enzymes showed similar substrate specificity for exogenous aldehydes and ketones and apparently absolute cofactor specificity for NADPH, their specificity for natural carbonyl compounds differed. The major form irreversibly reduced 5 alpha- and 5 beta-dihydrotestosterones, menadione and lauryl aldehyde with low Km values of 10-70 microM, whereas the minor form not only reduced 17-oxosteroids, of which 3 alpha-hydroxy-5 beta-androstan-17-one was the best substrate, but also oxidized 17-hydroxysteroids in the presence of NADP+. The two forms of carbonyl reductase also exhibited different sensitivity to heavy metal ions, dicoumarol, tetramethyleneglutaric acid, phenobarbitone and corticosteroids. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/6439186/Purification_and_characterization_of_two_forms_of_microsomal_carbonyl_reductase_in_guinea_pig_liver_ L2 - https://portlandpress.com/biochemj/article-lookup/doi/10.1042/bj2230697 DB - PRIME DP - Unbound Medicine ER -