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Partial purification and kinetic properties of ribose-5-phosphate ketol-isomerase and ribulose-5-phosphate 3-epimerase from various sources

1973; Elsevier BV; Volume: 293; Issue: 2 Linguagem: Inglês

10.1016/0005-2744(73)90360-4

1878-1454

Maureen E. Kiely, Allan L. Stuart, Terry Wood,

Metabolism, Diabetes, and Cancer

d-Ribose-5-phosphate ketol-isomerase (EC 5.3.1.6) was partially purified from calf spleen, calf liver and ox muscle. d-Ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) was prepared from calf liver. Mixtures of the isomerase and epimerase enzymes were separated by preparative electrophoresis in a 'Pevikon' block. Initial velocities of the isomerase and epimerase reactions were measured at 290 nm, at 340 nm, and by the cysteine carbazole method. The Km values for isomerase from spinach, spleen, muscle, and liver and for the epimerase from yeast and liver were determined. For spinach isomerase the Km values and the maximal velocities of both the forward and the reverse directions were measured.