Spectral properties of human placental aldose reductase and aldehyde reductase II.
Circular dichroism and fluorescence spectra of aldose reductase (E.C.1.1.1.21) and aldehyde reductase II (E.C.1.1.1.19) purified to homogeneity from human placenta have been studied. The alpha helical content of aldose reductase and aldehyde reductase II was 51% and 56%, respectively, whereas no beta helical structure was found in either case. In the case of aldose reductase, the secondary structure was unaffected at alkaline pH (9.5), whereas a drastic alteration in the structure was observed at 58 degrees C. The secondary structure of aldehyde reductase II, on the other hand, remained unaffected at higher pH and temperature.
Das
B
B
Department of Human Biological Chemistry & Genetics, University of Texas Medical Branch, Galveston 77550.
Bhatnagar
A
A
Liu
S Q
SQ
Srivastava
S K
SK
Messmer
M
M
Ueno
N
N
Chakrabarti
B
B
D000449:Aldehyde Reductase / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D002237:Carbohydrate Dehydrogenases; D002942:Circular Dichroism; D004795:Enzyme Stability; D005260:Female; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013401:Sugar Alcohol Dehydrogenases
D000596:Amino Acids; D002237:Carbohydrate Dehydrogenases; D013401:Sugar Alcohol Dehydrogenases; D000449:Aldehyde Reductase; C020843:gulonate dehydrogenase