A comparative study of the fixation of 75Se and 35S onto protein-polysaccharides of bovine costal cartilage

Campo, Robert D.; Wengert, Paul A.; Tourtelotte, Charles D.; Kirsch, Michael A.

doi:10.1016/0304-4165(66)90317-5

Cited by 7 publications

(1 citation statement)

References 23 publications

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“…It has been shown by Campo et al [1966Campo et al [ , 1967 that, in bovine costal cartilage, selenium is not incorporated into chondroitin sulfate, but is associated with a protein-polysaccharide as sociated with a protein.…”

Section: Discussionmentioning

confidence: 99%

Autoradiography of Selenium-75 in Developing Rat Teeth and Bone

Bawden¹,

Hammarström²

1977

Caries Res

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The distribution of sodium selenite ⁷⁵Se in young rats with special reference to teeth and bone has been studied by means of autoradiography. The highest concentrations of ⁷⁵Se were initially found in liver and intestine followed by kidney, circulating blood, and secretory mucosa of the stomach. Relatively high concentrations of ⁷⁵Se were found in the liver and kidney throughout the experimental period of 4 days. In calcifying tissues, a low to moderate concentration was found during the first few hours after injection. Among these tissues, the highest concentration was found in newly formed enamel matrix. 4 days after injection, most of the injected selenium had disappeared from the hard tissues.

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Section: Discussionmentioning

confidence: 99%

Autoradiography of Selenium-75 in Developing Rat Teeth and Bone

Bawden¹,

Hammarström²

1977

Caries Res

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Comparative Metabolism and Biochemistry of Selenium and Sulfur

Shamberger

1983

Biochemistry of Selenium

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Radioactive 75Se Labeling and Detection of Selenoproteins

Yim

Tobe

Turanov

et al. 2017

Methods in Molecular Biology

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The trace element selenium (Se) is incorporated into proteins as the amino acid selenocysteine (Sec), which is cotranslationally inserted into specific proteins in response to a UGA codon. Proteins containing Sec at these specific positions are called selenoproteins. Most selenoproteins function as oxidoreductases, while some serve other important functions. There are 25 known selenoprotein genes in humans and 24 in mice. The use of Sec allows selenoproteins to be detected by a convenient method involving metabolic labeling with Se. Labeling of cells and whole animals are used for the examination of selenoprotein expression profiles and the investigation of selenoprotein functions. In mammals, nonspecificSe insertion is very low, and sensitivity and specificity of selenoprotein detection approaches that of Western blotting. This method allows for the examination of selenoprotein expression and Se metabolism in model and non-model organisms. Herein, we describe experimental protocols for analyzing selenoproteins by metabolic labeling with Se both in vitro and in vivo. As an example, the procedure for metabolic labeling of HEK293T human embryonic kidney cells is described in detail. This approach remains a method of choice for the detection of selenoproteins in diverse settings.

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A comparative study of the fixation of 75Se and 35S onto protein-polysaccharides of bovine costal cartilage

Cited by 7 publications

References 23 publications

Autoradiography of Selenium-75 in Developing Rat Teeth and Bone

Autoradiography of Selenium-75 in Developing Rat Teeth and Bone

Comparative Metabolism and Biochemistry of Selenium and Sulfur

Radioactive 75Se Labeling and Detection of Selenoproteins

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