Immunochemical studies on malate dehydrogenase (decarboxylating) (NADP)

Isohashi, Fumihide; Shibayama, Kiyoko; Maruyama, Etsuko; Aoki, Yasuko; Wada, Fumio

doi:10.1016/0005-2744(71)90115-x

Cited by 31 publications

(10 citation statements)

References 19 publications

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“…The changes in enzyme activity resulting from alteration of physiological status, such as highsucrose feeding or treatment with thyroxine, are therefore due to changes in the amount of the same enzyme protein. A similar conclusion has been reported by Isohashi et al (1971).…”

Section: Homogeneity Of the Purified 'Malic' Enzymesupporting

confidence: 91%

“…An antiserum produced in our preliminary studies against a slightly impure preparation of hepatic 'malic' enzyme that has a specific activity of 16units/mg was found to react immunologically with kidney and brown adipose tissue, and in addition it gave a faint second band with spleen, kidney, intestinal mucosa and cardiac muscle. However, in agreement with Isohashi et al (1971) Full experimental details are given in the text. The antiserum (25 pl) or control serum was incubated with liver supernatant preparation from rats in various physiological conditions, as below, in a total volume of 2ml.…”

Section: Homogeneity Of the Purified 'Malic' Enzymesupporting

confidence: 76%

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Enzyme synthesis in the regulation of hepatic ‘malic’ enzyme activity

Murphy

Walker

1974

Biochemical Journal

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A homogeneous preparation of ;malic' enzyme (EC 1.1.1.40) from livers of thyroxine-treated rats was used to prepare in rabbits an antiserum to the enzyme that reacts monospecifically with the ;malic' enzyme in livers of rats in several physiological states. Changes in enzyme activity resulting from modification of the state of the animal are hence due to an altered amount of enzyme protein. The antiserum has been used to precipitate out ;malic' enzyme from heat-treated supernatant preparations of livers from both adult and neonatal rats, in a number of physiological conditions, that had been injected 30min earlier with l-[4,5-(3)H]leucine. The low incorporations of radioactivity into the immunoprecipitable enzyme have permitted the qualitative conclusion that changed enzyme activity in adult rats arises mainly from alterations in the rate of enzyme synthesis. The marked increase in ;malic' enzyme activity that occurs naturally or as a result of thyroxine treatment of the weanling rat is likewise due to a marked increase in the rate of enzyme synthesis possibly associated with a concurrent diminished rate of enzyme degradation.

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Section: Homogeneity Of the Purified 'Malic' Enzymesupporting

confidence: 91%

Section: Homogeneity Of the Purified 'Malic' Enzymesupporting

confidence: 76%

Enzyme synthesis in the regulation of hepatic ‘malic’ enzyme activity

Murphy

Walker

1974

Biochemical Journal

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“…It is well known, for example, that hepatic a-GPD fails to respond to T3 in human (56) and guinea pig (57) liver, despite the fact that this enzyme is an excellent index of thyroid hormone action in the rat. Moreover, it is apparent that T3 fails to stimulate either a-GPD or malic enzyme in brain (58); neither does T3 augment enzyme activity in heart (59) despite the fact that the structure of malic enzyme appears to be identical in these tissues (60).…”

Section: Some General Principles Of Thyroid Hormone Actionmentioning

confidence: 99%

Thyroid Hormone Action at the Cellular Level

Oppenheimer

1979

Science

501

169

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A large body of circumstantial evidence suggests that the basic unit of thyroid hormone action is the triiodothyronine nuclear receptor complex. This complex stimulates the formation, directly or indirectly, of a diversity of messenger RNA (mRNA) sequences. A generalized increase in mRNA as well as a disproportionate increase in a limited number of RNA sequences have been demonstrated. Regulation of thyroid hormone effects may be carried out largely at a local cellular level. Highly selective alterations in sensitivity to the triiodothyronine nuclear receptor complex may occur at specific target genes. Metabolic factors and hormones participate in such regulation. In a given tissue, alterations in the total number of receptor sites has not been shown to be useful as an index of thyroid hormone response, and local modulation of the response to the triiodothyronine receptor complex by a variety of factors other than triiodothyronine may be carried out at a postreceptor level.

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“…Hypothyroidism leads to a decrease in malic enzyme activity as com pared with controls, this effect being more significant in the enzyme from the soluble fraction than in the particulate fraction. It has been reported that the cytoplasmic malic enzyme from rat brain is immunochemically identical to the enzyme isolated from the liver [9]. This fact could explain why the cyto plasmic malic enzyme behaves more like the hepatic than like the mitochondrial enzyme.…”

Section: Resultsmentioning

confidence: 76%

Effect of Thyroid Hormones on the Malic Enzyme Activity in Rat Brain during Development

et al. 1981

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Changes in the developmental pattern of cytoplasmic and mitochondrial malate dehydrogenase (decarboxylating; NADP⁺) activity in the brain of hypothyroid rats and the effect of triiodothyronine on the enzyme activity have been investigated. Hypothyroid rats showed lower malate dehydrogenase activity than controls during the suckling period. Results suggest that thyroid hormones promote the development of malic enzyme in the brain.

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Immunochemical studies on malate dehydrogenase (decarboxylating) (NADP)

Cited by 31 publications

References 19 publications

Enzyme synthesis in the regulation of hepatic ‘malic’ enzyme activity

Enzyme synthesis in the regulation of hepatic ‘malic’ enzyme activity

Thyroid Hormone Action at the Cellular Level

Effect of Thyroid Hormones on the Malic Enzyme Activity in Rat Brain during Development

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