260
Views
19
CrossRef citations to date
0
Altmetric
Original Articles

A comparison of the metabolism of intravenously injected sodium selenite, sodium selenate, and selenomethionine in rats

, &
Pages 115-126 | Received 22 Aug 1972, Published online: 05 Jan 2012
 

Abstract

Rats were injected with Se75-sodium selenite, Se75-sodium selenate, and Se75-selenomethionine, and the distributions of Se75 in tissues, and in proteins isolated from plasma, liver supernatants, and kidney supernatants, were studied as a function of time.

The livers of rats injected with selenite had a much greater initial Se75 concentration than those from rats receiving selenate. Kidneys of rats injected with selenite had a peak Se75 concentration in the sample taken 1 hr after injection; this was followed by a rapid decline. Kidneys from rats injected with selenate had an almost constant Se75 level in all samples from 1 hr to 7 days. In other tissues the Se75 activities for rats injected with selenite were similar to those for rats injected with selenate. As has been reported elsewhere the tissues retaining the highest Se75 levels were the livers, kidneys, and adrenals.

Rats injected with selenomethionine contained greater Se75 concentrations in the pancreas than rats injected with selenite or selenate.

Dialysis of plasma and liver and kidney supernatants against isotonic saline showed that at 1 hr after injection selenomethionine was associated with protein to a greater extent than was selenite or selenate. Disulphide-cleaving reagents (mercaptoethanol and cysteine) and urea were effective in releasing Se75 from liver, kidney, and plasma proteins from rats injected with either selenomethionine, selenite, or selenate.

Se75 distribution patterns in liver, kidney, and plasma proteins separated by gel filtration or disc-electrophoresis were very similar for samples collected at 1 day, 3 days, and 7 days after injection of rats with either selenite, selenate, or selenomethionine. If, as has been proposed, selenium from selenite or selenate is present in protein as selenotrisulphide, this finding suggests that selenomethionine may not be incorporated into protein intact.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.