The 30 kDa protein co-purified with chick liver glutathione S-transferases is a carbonyl reductase.
An unidentified 30 kDa protein was co-purified with chick liver glutathione S-transferases from S-hexylglutathione affinity column. The protein was isolated to apparent homogeneity with chromatofocusing. The molecular mass of the protein was determined to be 30 277 +/- 3 dalton by mass spectrometry. The protein was digested with Achromobacter proteinase I. Amino-acid sequence analyses of the resulting peptides show a high degree of identity with those of human carbonyl reductase. The protein is active with menadione as substrate. Thus, it is identified as chick liver carbonyl reductase.
Tsai
S P
SP
Institute of Molecular Biolgoy, Academia Sinica, Taipei, Taiwan, R.O.C.
Wang
L Y
LY
Yeh
H I
HI
Tam
M F
MF
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification*; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008297:Male; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010449:Peptide Mapping; D017386:Sequence Homology, Amino Acid
D010446:Peptide Fragments; D000429:Alcohol Oxidoreductases; D005982:Glutathione Transferase