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J. Biol. Chem., Vol. 264, Issue 14, 7844-7849, May, 1989
TJ Huang, GM Trakshel and MD Maines
We have identified and characterized multiple forms of biliverdin reductase
(BVR) in control rat liver cytosol. Two-dimensional electrophoresis of the
purified BVR resolved a minimum of 10 discrete protein zones. All 10
proteins were BVR as judged by immunological cross-reactivity toward rabbit
anti-rat BVR. Based on the isoelectric focusing pattern of separation, the
BVR variants could be organized into five net-charge groups designated as
BVR-IEF1 to BVR-IEF5 and three molecular mass groups designated as
BVR-MW1-BVR-MW3, respectively. The pI values of the net-charge groups were:
BVR-IEF1, 6.23; IEF2, 5.91; IEF3, 5.76; IEF4, 5.61; IEF5, 5.48. The Mr
values of the molecular mass groups were: BVR-MW1, 30,400; MW2, 30,700;
MW3, 31,400. Single dimension slab gel isoelectric focusing offered greater
resolution of the net charge variants, and BVR-IEF3 was further resolved
into two variants, IEF3a and IEF3b, with pIs of 5.77 and 5.75,
respectively. The six net-charge variants also resolved on a preparative
chromatofocusing column and were designated as BVR-CF1-BVR- CF6. The pH
values of the peak fractions were: BVR-CF1, 6.91; CF2, 6.33; CF3, 6.03;
CF4, 5.82; CF5, 5.45; CF6, 5.27. Correspondence between the isoelectric
focusing net-charge variants and the chromatofocusing net-charge variants
was established. The Mr and net- charge variants did not represent
partially degraded forms of biliverdin reductase produced during
purification since the pattern of resolution of variants on slab gel
isoelectric focusing or two- dimensional electrophoresis did not change by
purifying the proteins in the presence of protease inhibitors and 5 mM
EDTA. BVR-CF2 and BVR-CF4 were purified and examined for pH-dependent
cofactor requirements for activity. Both net-charge variants and two pH
optima that were cofactor- dependent; maximum activity with NADPH, however,
was at pH 8.5 and with NADH at pH 6.7. With both variants, however, a
higher catalytic rate was observed with NADH than with NADPH at their
respective pH optima. Furthermore, BVR-CF2 exhibited a higher catalytic
rate than did BVR-CF4 with either cofactor throughout the pH range of 5-9.
Detection of 10 variants of biliverdin reductase in rat liver by two- dimensional gel electrophoresis
University of Rochester School of Medicine, Department of Biophysics, New York 14642.
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