Biochemical differences between cytoplasmic malate dehydrogenase allozymes of Drosophila virilis

Biochemical Genetics
S Narise

Abstract

Two allozymes (MDHf and MDHs) of cytoplasmic malate dehydrogenase of Drosophila virilis were partially purified and their biochemical properties were compared. MDHf has a pH optimum of 9.75 and MDHs one of 9.25 for malate oxidation. Optimal pH for oxaloacetate reduction is 6.75 and 8.0 for MDHf and MDHs, respectively. The Km value for oxaloacetate of MDHs is approximately twice as that of MDHf. No differences were found with respect to thermostability and Km's for malate, NAD+, or NADH. These results are discussed in terms of the physiological role of cytoplasmic malate dehydrogenase of D. virilis.

References

Jan 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·H RübsamenE Eigenbrodt
Sep 1, 1983·Evolution; International Journal of Organic Evolution·Pekka Pamilo

Citations

Apr 29, 1977·Documenta Ophthalmologica. Advances in Ophthalmology·P Nemet, S Ron
Apr 1, 1970·Biochemical Genetics·C R Shaw, R Prasad
Feb 11, 1970·Biochimica Et Biophysica Acta·M S McReynolds, G B Kitto
Apr 2, 1974·Archives of Biochemistry and Biophysics·N S Yang, J G Scandalios
May 16, 1967·Biochimica Et Biophysica Acta·G B Kitto, R G Lewis
Oct 1, 1968·Proceedings of the National Academy of Sciences of the United States of America·J Gillespie, K Kojima

Related Concepts

Oxaloacetates
Malate Dehydrogenase
Protoplasm
Oxaloacetate
Drosophila
NADH
Oxidation
Drosophila virilis
Cytoplasmic
Malate

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