Isolation, Purification, and Properties of Peroxisomal Malate Dehydrogenase from Maize Mesophyll

Isolation, Purification, and Properties of Peroxisomal Malate Dehydrogenase from Maize Mesophyll Peroxisomal malate dehydrogenase (EC 1.1.1.37) with a specific activity of 533 U/mg (144-fold purification) and a yield of 5% was obtained in a homogeneous state by a purification scheme including sucrose gradient centrifugation from maize mesophyll. The Michaelis constants for the forward and reverse reactions were determined to be 11.6 mM and 256 μM, and the pH optimum was 9.5 and 9.0, respectively. Analysis of the molecular weight of the native enzyme and its subunits showed that the peroxisomal malate dehydrogenase was a homodimer. It was established that the isolated and purified isoform of the enzyme had a higher affinity for malate and NAD+ in comparison with the mitochondrial and cytoplasmic isoforms. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Isolation, Purification, and Properties of Peroxisomal Malate Dehydrogenase from Maize Mesophyll

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Publisher
Pleiades Publishing
Copyright
Copyright © 2018 by Pleiades Publishing, Inc.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
D.O.I.
10.1134/S0003683818030031
Publisher site
See Article on Publisher Site

Abstract

Peroxisomal malate dehydrogenase (EC 1.1.1.37) with a specific activity of 533 U/mg (144-fold purification) and a yield of 5% was obtained in a homogeneous state by a purification scheme including sucrose gradient centrifugation from maize mesophyll. The Michaelis constants for the forward and reverse reactions were determined to be 11.6 mM and 256 μM, and the pH optimum was 9.5 and 9.0, respectively. Analysis of the molecular weight of the native enzyme and its subunits showed that the peroxisomal malate dehydrogenase was a homodimer. It was established that the isolated and purified isoform of the enzyme had a higher affinity for malate and NAD+ in comparison with the mitochondrial and cytoplasmic isoforms.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Jun 1, 2018

References

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