Isozymes and genetic control of NADP-malate dehydrogenase in mice

Henderson, Nanine S.

doi:10.1016/0003-9861(66)90121-4

Cited by 112 publications

(29 citation statements)

References 22 publications

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“…The observation of extra-and intramitochondrial isozymes of (NADP) malate dehydrogenase in a variety of tissues extends earlier findings [6][7][8]201. The intracellular distribution of the enzyme appears to be in some cases organ-specific ( e .…”

Section: Discussionsupporting

confidence: 74%

“…Some years ago in our laboratory data were obtained, which suggested the existence also of an intramitochondrial (NADP) malate dehydrogenase in adrenal cortex, heart and kidney [6]. As shown by Henderson [7] in several tissues of mice and pig, this mitochondrial enzyme is electrophoretically different from that of the cytoplasm. I n a recent communication Simpson et al [8] described in adrenal cortex intra-and extramitochondrial (NADP) malate dehydrogenase with different chromatographic and catalytic properties.…”

mentioning

confidence: 99%

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Intra‐ and Extramitochondrial Isozymes of (NADP) Malate Dehydrogenase

Brdiczka

Pette

1971

European Journal of Biochemistry

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The intracellular distribution of (NADP) malate dehydrogenase (decarboxylating) was studied by means of fractional extraction of extra-and intramitochondrial enzymes in various tissues of mouse, rat, rabbit, guinea pig, pig, beef, sea gull and pigeon. Absolute activity levels of (NADP) malate dehydrogenase in the same tissues of different species vary greatly. I n white adipose tissue and adrenal medulla, (NADP) malate dehydrogenase is located exclusively within the extramitochondrial compartment. I n liver, 95 Ol0 of (NADP) malate dehydrogenase activity is extramitochondrial and only 5 Ol0 intramitochondrial. Mitochondria1 subfractionation reveals a location of this enzyme within the inner mitochondrial compartment. Brain, heart, adrenal cortex and kidney also contain extra-and intramitochondrial (NADP) malate dehydrogenase. I n kidney and adrenal cortex, the ratio of extra-and intramitochondrial isozymes varies between different species. I n heart, a relatively constant distribution is found, i. e. 30°/, of the enzyme activity is extramitochondrial and 70 Ol0 is intramitochondrial. Extra-and intramitochondrial (NADP) malate dehydrogenases show different electrophoretic mobility in all tissues examined and can be characterized as two distinct isoenzymes. Extra-and intramitochondrial isozymes of (NADP) malate dehydrogenase are probably related to different metabolic functions in various tissues, e. 9. extra-intramitochondrial hydrogen transfer (malate shuttle) or transhydrogenation reactions.

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Section: Discussionsupporting

confidence: 74%

mentioning

confidence: 99%

Intra‐ and Extramitochondrial Isozymes of (NADP) Malate Dehydrogenase

Brdiczka

Pette

1971

European Journal of Biochemistry

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“…Malic enzyme in the mouse is a case in point, since two allelic electrophoretic forms have been recognized in homozygotes (Henderson, 1966). In this report, we will present evidence bearing on its structure and synthesis, based on electrophoretic patterns obtained from (1) tissues of heterozygotes; (2) skeletal muscle heterokaryons of allophenic mice (Mintz, 1962a(Mintz, , 1962b(Mintz, , 1964(Mintz, , 1965(Mintz, , 1967Mintz and Baker, 1967); and (3) mixtures of enzyme types in vitro, after dissociation and reassociation.…”

Section: Introductionmentioning

confidence: 97%

“…It catalyzes the oxidative decarboxylation of malate to pyruvate and the decarboxylation of oxaloacetate to pyruvate. In the mouse, NADP-MDH occurs in the supernatant fraction of homogenates of many tissues, where Henderson (1966) observed one of two electrophoretic variants, in each of several inbred strains. The locus responsible for synthesis of the mouse supernatant enzyme is autosomal (Henderson, 1966) and has been designated Mdh-1, with the alleles Mdh-l" and Mdh-1 b.…”

Section: Introductionmentioning

confidence: 99%

Subunit structure and gene control of mouse NADP?malate dehydrogenase

Baker

Mintz

1969

Biochem Genet

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“…There are several isozyme differences between IR and BW5147, one of which is in malic enzyme (MES): IR has a slower migrating form than BW5147 (Henderson, 1966 These experiments show that it is possible to transfer the human chromosome carrying Ecogpt from attached to suspension cells. This may be a general way of introducing genes into specific cell types which are difficult to transfect by direct methods, such as calcium phosphate co-precipitation.…”

Section: Transfection Of Human Fibroblasts With Psv3-gptmentioning

confidence: 79%

Integration of Ecogpt and SV40 early region sequences into human chromosome 17: a dominant selection system in whole cell and microcell human-mouse hybrids.

Tunnacliffe¹,

Parkar²,

Povey³

et al. 1983

The EMBO Journal

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The dominant selectable gene, Ecogpt, has been introduced, by the calcium phosphate precipitation technique, into normal human fibroblasts, along with the SV40 early region genes. In one transfectant clone, integration of these sequences into human chromosome 17 was demonstrated by the construction of human‐mouse somatic cell hybrids, selected for by growth in medium containing mycophenolic acid and xanthine. A whole cell hybrid, made between the human transfectant and a mouse L cell, was used as donor of the Ecogpt‐carrying human chromosome 17 to ‘tribrids’ growing in suspension, made by whole cell fusion between a mouse thymoma cell line, and to microcell hybrids made with a mouse teratocarcinoma cell line. Two tribrids contained karyotypically normal human chromosomes 17 and a small number of other human chromosomes, while a third tribrid had a portion of the long arm of chromosome 17 translocated to mouse as its only human genetic material. Two independent microcell hybrids contained a normal chromosome 17 and no other human chromosome on a mouse teratocarcinoma background. These experiments demonstrate the ability to construct human‐mouse somatic cell hybrids using a dominant selection system. By applying this approach it should be possible to select for a wide range of different human chromosomes in whole cell and microcell hybrids. In particular, transfer of single human chromosomes to mouse teratocarcinoma cells will allow examination of developmentally regulated human gene sequences after differentiation of such hybrids.

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Isozymes and genetic control of NADP-malate dehydrogenase in mice

Cited by 112 publications

References 22 publications

Intra‐ and Extramitochondrial Isozymes of (NADP) Malate Dehydrogenase

Intra‐ and Extramitochondrial Isozymes of (NADP) Malate Dehydrogenase

Subunit structure and gene control of mouse NADP?malate dehydrogenase

Integration of Ecogpt and SV40 early region sequences into human chromosome 17: a dominant selection system in whole cell and microcell human-mouse hybrids.

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