PMID: 2108605Apr 1, 1990Paper

Chromatographic separation of activated and unactivated forms of aldose reductase

Archives of Biochemistry and Biophysics
C E Grimshaw

Abstract

Chromatography of bovine kidney aldose reductase using Matrex Orange A affinity gel results in the separation of the unactivated and activated enzyme forms. The former washes through the column, while the latter is eluted with an NADPH step-gradient. The separated enzyme forms display Vmax and Km glycolaldehyde values, and relative sensitivities to inhibition by the aldose reductase inhibitor AL-1576 (spiro[2,7-difluorofluorene-9,4'-imidazolidine]-2',5'- dione), that are similar to those reported previously for the individual forms. However, because Vmax is 17-fold lower for the unactivated enzyme, the purification of aldose reductase via NADP(H) elution from a dye-ligand affinity matrix can result in the selective purification of only the activated enzyme form. These results have direct implications for the study of potential aldose reductase inhibitors, and may explain why linear double-reciprocal plots are commonly observed for enzyme prepared in this manner, while nonlinear plots are seen in other cases.

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Citations

Aug 1, 1993·The International Journal of Biochemistry·M OhtaT Hayakawa
Apr 1, 1994·The International Journal of Biochemistry·M OhtaT Hayakawa
Apr 17, 1992·Biochimica Et Biophysica Acta·S Q LiuS K Srivastava
Sep 20, 1996·Journal of Chromatography. B, Biomedical Applications·F ToribioJ López-Barea
Feb 19, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·P MayrB Nidetzky
Oct 1, 1992·Biochemical Medicine and Metabolic Biology·A Bhatnagar, S K Srivastava
Mar 29, 2006·The Journal of Biological Chemistry·Karin KaiserovaAruni Bhatnagar
Jan 5, 2002·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Yuying C HwangRavichandran Ramasamy

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