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Isolation of the flavodehydrogenase domain of hansenula anomala flavocytochrome b 2 after mild proteolysis by a hansenula anomala proteinase



Isolation of the flavodehydrogenase domain of hansenula anomala flavocytochrome b 2 after mild proteolysis by a hansenula anomala proteinase



European Journal of Biochemistry 182(1): 67-76



The protomeric chain of Hansenula anomala flavocytochrome b2 was previously shown to be built as the covalent association of two functional domains: an L-lactate dehydrogenase domain and a cytochrome c reductase domain, joined together by a proteolytically sensitive zone. This paper concerns the specific cleavage of this latter zone with a H. anomala proteinase(s) preparation and the purification of the resulting L-lactate dehydrogenase moiety of the molecule with at least 25% recovery, (i.e. one order of magnitude more than for the previously published method). A preliminary characterization of this dehydrogenase domain indicates that it is a tetramer (Mr = 4 .times. 39000) containing FMN as expected and not heme. It has high L-lactate:ferricyanide oxidoreductase activity (about 70% that of the whole flavocytochrome b2) and the same Km for L(+)-lactate as flavocytochrome b2. The subcellular origin of the H. anomala proteinase in the preparation has not yet been elucidated.

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