Purification and properties of sorbitol dehydrogenase from mouse liver

Burnell, James N.; Holmes, Roger S.

doi:10.1016/0020-711x(83)90124-6

Cited by 16 publications

(3 citation statements)

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“…Sorbitol dehydrogenase (SDH; L-iditol:NAD+ 2-oxidoreductase; EC 1.1.1.14) has been purified from a variety of sources. Because the enzyme is most abundant in mammalian liver, structural analyses of purified SDH from mouse (Burnell and Holmes, 1983), sheep (Jeffery et al, 1984a), and human (Maret and Auld, 1988) liver have been undertaken. The finding of one zinc atom per subunit of the tetrameric enzyme (Jeffery et al, 1984b) and elucidation of the primary structure (Jeffery et al, 1984a) of the sheep liver enzyme led to the proposal of a close evolutionary relationship between alcohol and polyol dehydrogenases (Eklund et al, 1985;Jornvall et al, 1987).…”

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confidence: 99%

Purification and Characterization of Sorbitol Dehydrogenase from Bovine Brain

Wiesinger

Hamprecht

1989

Journal of Neurochemistry

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Sorbitol dehydrogenase (EC 1.1.1.14) was isolated from bovine brain and purified 3,000-fold to apparent homogeneity, as judged by polyacrylamide gel electrophoresis. The purified enzyme had a specific activity of 36 units/mg of protein; a molecular weight of 39,000 for each of the four identical subunits and 155,000 for the intact enzyme were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel exclusion chromatography, respectively. The presence of one Zn2+ per subunit was confirmed by atom absorption spectroscopy; inactivation of the enzyme by metal-chelating agents points to the essential role that Zn2+ plays in the catalytically competent enzyme. The enzyme is also inactivated by thiol-blocking reagents; with respect to inactivation by sodium pyrophosphate, sorbitol dehydrogenase is different from closely related alcohol dehydrogenase.

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confidence: 99%

Purification and Characterization of Sorbitol Dehydrogenase from Bovine Brain

Wiesinger

Hamprecht

1989

Journal of Neurochemistry

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“…Sorbitol dehydrogenase cloning and sequence analysis. Sorbi-to1 dehydrogenase from various species including human, rat, sheep, cow, and mouse have similar molecular masses, subunit components, and specific activities (Burnell and Holmes, 1983). The amino acid sequence deduced from the coding region of MSD7 shows high similarity with the sequence of sorbitol dehydrogenase from human (Karlsson et al, 1989;Lee et al, 1994), sheep (Jeffery et al, 1984a), and rat (Karlsson et al, 1991), indicating that it is a clone of the mouse sorbitol dehydrogenase cDNA.…”

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confidence: 96%

Cloning, Sequencing, and Determination of the Sites of Expression of Mouse Sorbitol Dehydrogenase cDNA

Lee¹,

Lee²,

Lin³

et al. 1995

European Journal of Biochemistry

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Sorbitol dehydrogenase is one of the enzymes in the polyol pathway, which is thought to be implicated in the pathogenesis of diabetic complications. The cDNA encoding mouse sorbitol dehydrogenase was cloned from a liver library and its sequence was determined. The open reading frame encodes a product of 356 amino acids that shares high similarity with the human and rat liver sorbitol dehydrogenases (83% and 93% identity, respectively). The 3′‐untranslated region contains a truncated L1Md repeat element inserted in reverse relative to the sorbitol dehydrogenase cDNA. Northern‐blot hybridization showed that the testis has the highest level of expression, followed by kidney, liver, and lung. Low levels of expression were also observed in lens, brain, and skeletal muscle. In situ hybridization revealed that in the kidney, the highest concentration of sorbitol dehydrogenase mRNA is observed in the cortex, but is absent from the inner medulla. The parenchymal cells of the liver showed strong expression while the cells of the hepatic vasculature did not hybridize. The sorbitol dehydrogenase expression in the seminiferous tubules was mostly associated with the mature cells of the developing germ cells, confirming the usefulness of sorbitol dehydrogenase as an enzyme indicator for sexual maturation. The seminal vesicle, where most of the seminal fructose is produced, also showed a high level of expression in the epithelial cells. The mouse sorbitol dehydrogenase cDNA will be useful in the studies of the involvement of the polyol pathway in diabetic complications.

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“…Sorbitol dehydrogenase enzyme is also a member of the polyol dehydrogenase family. Sorbitol dehydrogenase (NAD ＋ oxidoreductase) is one of the two enzymes of the polyol pathway called the sorbitol pathway, which catalyzes the alternating oxidation-reduction reaction between sorbitol and fructose and uses NAD ＋ as a coenzyme 12) .…”

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Anti-lung Cancer, Anti-microbial, Anti-α-glucosidase, Anti-sorbitol Dehydrogenase, and <i>in silico</i> Studies of Wogonoside and Isoliquiritigenin as Natural Compounds

Zeng,

Zhao,

Yao

2023

J. Oleo Sci.

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Cancer is one of the most dangerous diseases responsible for the death of more than a third of the world s population. Cancer manifests itself in certain forms determined by uncontrolled cell proliferation in all its types. Cancer is a large family of diseases caused by cells that have uncontrolled division ability to spread to other parts of the body. These uncontrolled cells called neoplasms form cell piles or tubers called tumors. Uncontrolled division ability is not the only distinctive property of cancer cells. The properties of these abnormal cells that differ in terms of cellular and molecular metabolism are explained in detail by Hannahan and Weinberg 1) . Stating that there are 6 hallmarks of #

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Purification and properties of sorbitol dehydrogenase from mouse liver

Cited by 16 publications

References 16 publications

Purification and Characterization of Sorbitol Dehydrogenase from Bovine Brain

Purification and Characterization of Sorbitol Dehydrogenase from Bovine Brain

Cloning, Sequencing, and Determination of the Sites of Expression of Mouse Sorbitol Dehydrogenase cDNA

Anti-lung Cancer, Anti-microbial, Anti-α-glucosidase, Anti-sorbitol Dehydrogenase, and <i>in silico</i> Studies of Wogonoside and Isoliquiritigenin as Natural Compounds

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