A characterization of volatile carbonyl compounds isolated from meat fat subjected to gamma radiation

1958 ◽  
Vol 35 (8) ◽  
pp. 413-416 ◽  
Author(s):  
L. A. Witting ◽  
B. S. Schweigert
2020 ◽  
Vol 108 ◽  
pp. 110209
Author(s):  
Malik H. Mahmood ◽  
László Himics ◽  
László Péter ◽  
Péter Baranyai ◽  
Miklós Veres
Keyword(s):  

IEEE Access ◽  
2020 ◽  
Vol 8 ◽  
pp. 139479-139488
Author(s):  
Naif Mohammed Al-Hada ◽  
Abbas M. Al-Ghaili ◽  
Hairoladenan Kasim ◽  
Muneer Aziz Saleh ◽  
Elias Saion ◽  
...  

1984 ◽  
Vol 223 (3) ◽  
pp. 697-705 ◽  
Author(s):  
S Usui ◽  
A Hara ◽  
T Nakayama ◽  
H Sawada

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.


1977 ◽  
Vol 72 (2) ◽  
pp. 277
Author(s):  
R. S. Jaenke ◽  
R. D. Phemister ◽  
G. M. Angleton ◽  
D. D. Davis
Keyword(s):  

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