Mechanism of malate dehydrogenase isoform formation in <Emphasis Type="Italic">Sphaerotilus natans</Emphasis> D-507 under different cultivation conditions |
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Authors: | A T Eprintsev M I Falaleeva M A Arabtseva I A Lavrinenko I V Parfenova M V Grechkina F S Abud |
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Institution: | (1) Department of Microbiology III, Faculty of Biology, University Complutense of Madrid, Madrid, Spain; |
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Abstract: | Electrophoretically homogenous preparations of malate dehydrogenase (MDH) isoforms of the bacteria Sphaerotilus natans D-507 with specific activity 7.46 U/mg and 5.74 U/mg with respect to protein concentration have been obtained. The dimeric
isoform of the enzyme was shown to function under organotrophic growth conditions, whereas the tetrameric isoform was induced
under mixotrophic cultivation conditions. PCR-analysis revealed a single gene encoding the malate dehydrogenase molecule.
The topography of the MDH isoform surface was studied by atomic-force microscopy, and a 3D-structure of the enzyme was obtained.
Spectraphotometric analysis data allowed us to suggest that stabilization of the tetrameric form of MDH is due to additional
bounds implicated in the quaternary structure formation. |
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