Sod

Sod or turf is grass and the part of the soil beneath it held together by the roots, or a piece of thin material.

In British English such material is more usually known as turf, and the word "sod" is limited mainly to agricultural senses (for example for turf when ploughed).

Uses

Sod is typically used for lawns, golf courses, and sports stadiums around the world. In residential construction, it is sold to landscapers, home builders or home owners who use it to establish a lawn quickly and avoid soil erosion. Sod can be used to repair a small area of lawn, golf course, or athletic field that has died. Sod is also effective in increasing cooling, improving air and water quality, and assisting in flood prevention by draining water.

Scandinavia has a long history of employing sod roofing and a traditional house type is the Icelandic turf house.

Following passage of the Homestead Act by the US Congress in 1862, settlers in the Great Plains used sod bricks to build entire sod houses. While it might be hard for some to imagine sod as a suitable primary building material, the prairie sod of the Great Plains was so dense and difficult to cut it earned the nickname Nebraska marble. Blacksmith John Deere made his fortune when he became the first to make a plow that could reliably cut the prairie sod.

Sod (disambiguation)

Sod is grass and the part of the soil beneath it held together by the roots.

Sod may also refer to:

SOD or S.O.D. may refer to:

Science

Entertainment

Other uses

See also

SOD1

Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or SOD1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases. It is implicated in apoptosis and amyotrophic lateral sclerosis.

Structure

SOD1 is a 32 kDa homodimer which forms a β-barrel and contains an intramolecular disulfide bond and a binuclear Cu/Zn site in each subunit. This Cu/Zn site holds the copper and a zinc ion and is responsible for catalyzing the disproportionation of superoxide to hydrogen peroxide and dioxygen. The maturation process of this protein is complex and not fully understood, involving the selective binding of copper and zinc ions, formation of the intra-subunit disulfide bond between Cys-57 and Cys-146, and dimerization of the two subunits. The copper chaperone for Sod1 (CCS) facilitates copper insertion and disulfide oxidation. Though SOD1 is synthesized in the cytosol can mature there, the fraction of expressed, and still immature, SOD1 targeted to the mitochondria must be inserted into the intermembrane space. There, it forms the disulfide bond, though not metallation, required for its maturation. The mature protein is highly stable, but unstable when in its metal-free and disulfide-reduced forms. This manifests in vitro, as the loss of metal ions results in increased SOD1 aggregation, and in disease models, where low metallation is observed for insoluble SOD1. Moreover, the surface-exposed reduced cysteines could participate in disulfide crosslinking and, thus, aggregation.