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Protoplasma : Volume 207, Issue 1-2, March 1999

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Plasma-membrane-bound malate dehydrogenase activity in maize roots

Content Provider	Springer Nature Link
Author	Hadži Taskovišković, V. Vuletić, M. Ignjatović Micić, D. Vučinić, Ž.
Copyright Year	1999
Abstract	Plasma membranes were isolated and purified from 14-day-old maize roots (Zea mays L.) by two-phase partitioning at a 6.5% polymer concentration, and compared to isolated mitochondria, microsomes, and soluble fraction. Marker enzyme analysis demonstrated that the plasma membranes were devoid of cytoplasmic, mitochondrial, tonoplast, and endoplasmic-reticulum contaminations. Isolated plasma membranes exhibited malate dehydrogenase activity, catalyzing NADH-dependent reduction of oxaloacetate as well as NAD+-dependent malate oxidation. Malate dehydrogenase activity was resistant to osmotic shock, freeze-thaw treatment, and salt washing and stimulated by solubilization with Triton X-100, indicating that the enzyme is tightly bound to the plasma membrane. Malate dehydrogenase activity was highly specific to NAD+ and NADH. The enzyme exhibited a high degree of latency in both right-side-out (80%) and inside-out (70%) vesicle preparations. Kinetic and regulatory properties with ATP and Pi, as well as pH dependence of plasma-membrane-bound malate dehydrogenase were different from mitochondrial and soluble malate dehydrogenases. Starch gel electrophoresis revealed a characteristic isozyme form present in the plasma membrane isolate, but not present in the soluble, mitochondrial, and microsomal fractions. The results presented show that purified plasma membranes isolated from maize roots contain a tightly associated malate dehydrogenase, having properties different from mitochondrial and soluble malate dehydrogenases.
Starting Page	203
Ending Page	212
Page Count	10
File Format	PDF
ISSN	0033183X
Journal	Protoplasma
Volume Number	207
Issue Number	3-4
e-ISSN	16156102
Language	English
Publisher	Springer-Verlag
Publisher Date	1999-01-01
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ferricyanide reductase Isozyme form Plasma membrane Malate dehydrogenase Oxaloacetate Root Zea mays L Cell Biology Plant Sciences Zoology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine

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