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  • Title: Purification and electrospray mass spectrometry of aldose reductase from pig lens.
    Author: Reymann JM, Rondeau JM, Barth P, Jaquinod M, Van Dorsselaer A, Biellmann JF.
    Journal: Biochim Biophys Acta; 1992 Jul 13; 1122(1):1-5. PubMed ID: 1633191.
    Abstract:
    Aldose reductase (alditol: NADP+ 1-oxidoreductase, EC 1.1.1.21) has been purified from pig lens to homogeneity by a rapid and efficient three-step procedure involving poly(ethylene glycol) fractionation, ion-exchange chromatography and chromatofocusing. The homogeneity of the purified enzyme was examined by polyacrylamide gel electrophoresis under native and denaturing conditions, by isoelectric focusing and by high-performance liquid chromatography on a size-exclusion column. The highly purified enzyme is a monomeric protein with a molecular mass of 35,775 +/- 3 Da as determined by electrospray mass spectrometry (ESMS). This purification procedure is particularly suited for the preparation of triclinic single crystals of pig lens aldose reductase, which are currently used in X-ray studies of this enzyme.
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