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PubMed1975

75Se-selenomethionine-labeled lipoproteins in hyperlipidemic and normolipidemic humans.

Investigating the feasability and application appropriate to determination of lipoprotein turnover, 75Se-selenomethionine (Se-M) incorporation in lipoproteins was studied in eight hospitalized patients. Three were hyperlipidemic diabetic subjects (HL), and five were normolipidemic but otherwise abnormal subjects (NL). Maximum activity was observed in the VLDL fraction within 2-3 hr, and was followed by a biexponential decay. Incorporation into the LDL-I (density, 1.006-1.019 mug/ml) occurred at a rate which correlated with the rapid decay rate of the VLDL Se-M activity. The decay of the Se-M was single exponential in the LDL-I and LDL-II (density, 1.019-1.063 mug/ml), suggesting undirectional transfer of the label. The HDL fraction showed a rapid initial Se-M uptake which was followed by a slow rise, resulting in a complex time-activity curve. The Se-M activity was significantly higher in the VLDL fraction and slightly lower in the LDL and HDL fractions in the HL as compared to the NL subjects. The VLDL-apoprotein concentration increased by a significantly greater amount in the HL (374 mug/ml) than in the NL subjects (67 mug/ml). There was a significant increase in VLDL-apoprotein turnover in the presence of a fractional turnover rate that was not significantly lower in the three hyperlipidemic subjects compared to the NL controls. In vivo 75Se-selenomethionine labeling allows the estimation of the synthesis and removal rate of apoproteins.

Adult↗
PubMed1987

Trimethylselenonium ion.

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Chromatography, High Pressure Liquid↗
PubMed1995

Selenophosphate.

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Anaerobiosis↗
PubMed1988

Selenium-containing proteins of rat kidney.

Rat kidney selenium (Se)-containing proteins were studied by isotopic labeling with [75Se]selenite or [75Se]selenomethionine via three routes: oral, intraperitoneal injection, and incubation of kidney slices with the isotope. The two major Se-containing proteins in kidney were fractionated and partially characterized. 75Se elution profiles from Sephadex G-150 chromatography were similar for each labeling protocol, except for the profile obtained following incubation of slices with [75Se]selenomethionine. Of the two major 75Se-containing proteins, the one eluting at the void volume during Sephadex G-150 fractionation had a subunit of 23,000 Mr. The 75Se-labeled tryptic peptide from this protein and a 75Se-containing tryptic peptide from glutathione peroxidase had the same elution time from an HPLC column. A 75,000 Mr 75Se-containing protein had a 65,000 Mr subunit, and the 75Se-labeled tryptic peptide from this protein eluted from the HPLC column before that of glutathione peroxidase. Glutathione peroxidase is the most abundant kidney selenoprotein. Injection of animals with 75Se is the method of choice for isotopic labeling of rat kidney Se-containing proteins. Appropriate methods were developed that can be used in future studies of kidney Se-containing proteins.

Animals↗
PubMed1988

Glutathione peroxidase activity and chemical forms of selenium in tissues of rats given selenite or selenomethionine.

Glutathione peroxidase (GPx) activity and deposition of selenium (Se) were examined in tissues of rats given dietary Se for 7 wk as either selenite or selenomethionine (SeMet) with 75Se radiotracer of the same chemical form. On the basis of Se:75Se ratio, all tissues of the rats fed selenite were equilibrated with the dietary source, but tissues of the SeMet fed animals maintained a ratio of Se:75Se greater than the dietary ratio. Deposition of dietary Se and 75Se was higher in most tissues of rats fed SeMet. Muscle 75Se was the largest single tissue pool of 75Se in both groups accounting for one-third of recovered 75Se in the rats fed selenite, and one-half of recovered 75Se in the rats fed SeMet. Tissue GPx activities were not different between the two dietary groups. The proportion of Se as GPx in tissues was highest in erythrocytes of the rats fed selenite (.81) and lowest in testes and epididymides of the rats fed SeMet (.009). The proportion of Se present in cytosolic GPx was consistently higher in tissues of rats fed selenite. Erythrocytes of the rats fed SeMet had more 75Se associated with hemoglobin, and muscle cytosols of the rats fed selenite had more 75Se associated with the G-protein. The proportion of 75Se as SeMet determined by ion exchange chromatography of tissue hydrolysates was higher in tissues of rats fed SeMet (highest in muscle and hemoglobin, 70%, and lowest in testes, 16%). In contrast, selenocysteine was the predominant form of Se present in tissues of rats given selenite. These results indicate that the form of Se administered will influence the form in the tissues, the percentage of Se with GPx and the body burden of Se.

Animals↗