Crystallization and properties of rat liver malate dehydrogenase (decarboxylating) (NADP+)

Wada, Fumio; Numata, N.; Eguchi, Y.; Sakamoto, Yukiya

doi:10.1016/0005-2744(75)90225-9

Cited by 18 publications

(1 citation statement)

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“…Whereas the isoelectric point of bovine brain mME is 6.9 (authors' unpublished data), a zero net charge was fciund on cME at pH 6.2 in this study. This value compares well with isoelectric points of 6.3 and 6.15 determined for the cytosolic enzymes isolated from rat liver (Wada et al, 1975) and rat skeletal muscle (Swierczyhski, 1980), respectively. The different molecular masses and isoelectric points of cME and mME are further indications of structural differences of the two ME isozymes from bovine brain.…”

Section: Discussionsupporting

confidence: 85%

Purification of Cytosolic Malic Enzyme from Bovine Brain, Generation of Monoclonal Antibodies, and Immunocytochemical Localization of the Enzyme in Glial Cells of Neural Primary Cultures

Kurz

Wiesinger

Hamprecht

1993

Journal of Neurochemistry

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Cytosolic malic enzyme (EC 1.1.1.40) was purified from bovine brain 5,600-fold to a specific activity of 47 U/mg. The enzyme is a homotetramer with a subunit molecular mass of 60 kDa and an isoelectric point of 6.2. Mouse monoclonal antibodies raised against this enzyme were purified and shown to be monospecific, as indicated by immunoblotting. Immunocytochemical examination of rat astroglia-rich primary cultures at the light microscopic level revealed colocalization of cytosolic malic enzyme with the astroglial marker glial fibrillary acidic protein. Also, a colocalization with the oligodendroglial marker myelin basic protein was found. Neurons in rat neuron-rich primary cultures did not show positive staining. The data suggest that cytosolic malic enzyme is a glial enzyme and is lacking in neurons.

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Section: Discussionsupporting

confidence: 85%