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Molecular forms of biliverdin reductase from rat liver with different reduction rates for biliverdin-IX

1982; Elsevier BV; Volume: 105; Issue: 2 Linguagem: Inglês

10.1016/0006-291x(82)91498-x

1090-2104

Rosalía B. Frydman, Marı́a L. Tomaro, Josefina Awruch, Benjamín Frydman,

Hemoglobin structure and function

Biliverdin reductase from normal rat liver was separated into two forms by DEAE-cellulose. The major component (peak 1) had the properties ascribed to purified biliverdin reductase of rat liver. It reduced biliverdin-IXα at the highest rate, while it had a lower affinity for the other three biliverdin isomers. The minor component (peak 2) reduced biliverdin-IXβ at a rate similar to that of biliverdin-IXα, and its molecular and kinetic properties are different from those of peak 1. When the rats were pretreated with CoCl2, peak 2 remained unchanged, while the major peak 1 dissappeared and was replaced by a new major form (peak 3) which reduced biliverdin-IXβ at the highest rate and biliverdin-IXα at a slightly lower rate. The molecular form 3 of biliverdin reductase differed from the other two forms of the enzyme in its molecular and enzymatic properties.