Selenium

Name: Selenium
Brand: Springer Nature
SKU: 9780387338279
Availability: InStock

Best Price (Coupon Required):
Buy Selenium for $36.00 at @ Link.springer.com when you apply the 10% OFF coupon at checkout.
Click “Get Coupon & Buy” to copy the code and unlock the deal.

Set a price drop alert to never miss an offer.

1 Offer Price Range: $39.99 - $39.99

BEST PRICE

Single Product Purchase

$36.00

@ Link.springer.com with extra coupon

Price Comparison

Seller	Contact Seller	List Price	On Sale	Shipping	Best Promo	Final Price	Volume Discount	Financing	Availability	Seller's Page
BEST PRICE 1 Product Purchase @ Link.springer.com		$39.99	$39.99		10% OFF This deals requires coupon	$36.00		See Site	In stock	Visit Store

Product Details

Brand

Springer Nature

Manufacturer

N/A

Part Number

GTIN

9780387338279

Condition

New

Product Description

The discovery of selenoproteins in 1973 was the starting point for today's flourishing selenium field [1,2]. It provided evidence that selenium had biochemical functions that could account for its nutritional effects [3,4]. Further, it opened the selenium field to investigation by the methods of biochemistry, which led to the identification of several more selenoproteins and showed that selenocysteine was the form of the element in animal selenoproteins and in most bacterial ones. Although noteworthy efforts were made to uncover the mechanism of selenocysteine and selenoprotein synthesis using biochemical methods, the problem yielded only when attacked with the methods of molecular biology [5,6]. The bacterial mechanism was characterized first; characterization of the animal mechanism is a work in progress. It is interesting to note that the only genes that are devoted to selenium metabolism are those that support selenoprotein synthesis and selenocysteine catabolism. Consequently, it seems likely that competition for selenium between selenoprotein synthesis and the production of selenium excretory metabolites [7] controls who- body selenium homeostasis. The physiological functions of selenium derive fi-om the catalytic and physical properties of selenoproteins. Selenoproteins such as the glutathione peroxidases and the thioredoxin reductases have redox activities that allow them to serve in oxidant defense. The deiodinases use their redox activities to activate and inactivate thyroid hormones. From these two examples, it can be seen that selenoprotein functions are diverse while having in common a redox mechanism.

Available Colors

N/A

Available Sizes

N/A