LII.—ββ′-Dichlorodiethyl disulphide

Protein disulphide-isomerase and the formation of native disulphide bonds.

Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be regarded as a key post-translational modification of secretory proteins. Despite this, and despite the fact that the existence of disulphide bonds has been known for many years, the mechanism of disulphide bond formation during protein biosynthesis and secretion is not w...

NADPH-dependent disulphide reductases.

15. Olive, C., Geroch, M. E. & Levy, H. R. ( 197 1 ) J. Biol. Chem. 246,2047-2057 Levy, H. R. & Daouk, G. H. (1979) J. Biol. Chem. 254, 4843-4847 Grove, T. H., Ishaque, A. & Levy, H. R. ( I 976) Arch. Biochem. Biophys. 177,307-316 Levy, H. R., Christoff, M., Ingulli, J. & Ho, E. M. L. ( 1 983) Arch. Biochem. Biophys. 222,473-488 Levy, H. R.. Daouk, G. H. & Katopes, M. A. (1979) Arch. Riochem. B...

Disulphide interchange reactions.

Protein disulphide isomerase

What is it? Protein disulphide isomerase is an enzyme with two interrelated activities: as an oxidoreductase, it can catalyse the formation, reduction and isomerisation of disulphide bonds; and as a polypeptide binding protein, it can function as a molecular chaperone which assists the folding of polypeptides. Transient association of PDI with nascent polypeptides during their folding prevents ...

Tungsten disulphide sheathed carbon nanotubes.

An insulated nanotube wire is formed by the binary phase of layered tungsten disulphide and carbon nanotubes (shown in the HRTEM image) generated by the sulphidization of tungsten oxide coated multiwalled carbon nanotubes at 900 °C. Thermogravimetric analysis shows that the tungsten disulphide coat acts as an antioxidant.