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J. Biochem, 1992, Vol. 112, No. 6 849-855
© 1992 Japanese Biochemical Society

research-article

Purification and Characterization of Monomeric Isocitrate Dehydrogenase with NADP+-Specificity from Vibrio parahaemolyticus Y-4

Noriyuki Fukunaga1, Sigeki Imagawa2, Takehiko Sahara, Atsushi Ishii3 and Masahiro Suzuki

Department of Biology, Faculty of Science, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

1 To whom correspondence should be addressed

NADP+-dependent isocitrate dehydrogenase [IDH: EC 1.1.1.42 [EC] ] was purified to electro-phoretic homogeneity from Vibrio parahaemolyticus Y-4, and shown to be a monomeric protein of molecular weight 80,000 with a pi of 5.0. The amino acid composition and partial sequence at the N-terminus resembled those reported for other bacterial monomeric IDHs. Immunotitration with antisera to the monomeric and dimeric enzymes (antisera to EDH-II and -I of Vibrio ABE-1) showed an immunochemical distinction between the monomeric and dimeric IDHs, but there is similarity within the IDHs of each group. The circular dichroism spectra of the native and heat-denatured enzyme are also similar to those of monomeric IDH (H)H-II of Vibrio ABE-1). These monomeric IDHs are proteins comprising 17–22% helix and 25–35% ß-pleated sheet in the native state.

2Present addresses: Niigata Research Laboratory, Mitsubishi Gas Co., Niigata 950-31

3Group on Neuropharmacology, Faculty of Pharmacy, Josai University, Sakado, Saitama 350-02.


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