Hydrophobic Character of Ca^<2+>-bound S-100 Complexes

The hydrophobic character of thiol-activated cytolysins.

Hydrophobic chromatography on phenyl-Sepharose has revealed the decidedly hydrophobic character of several members of the group of cytolytic proteins termed ;thiol-activated'. Pneumolysin, alveolysin, cereolysin, and streptolysin O were found to be equally hydrophobic, as were the oxidized and reduced forms of alveolysin. Hydrophobic chromatography has been utilized in the development of an imp...

The Hydrophobic Character of Pretreated Coal Surfaces

partially replace oil and natural gas as fuel sources. Of all the coal-cleaning pmesses, flotation is one. of the most versatile. Carbon dioxide coal flotation is a new technology developed at the University of Utah.(l) Compared with conventional flotation, carbon dioxide flotation enhances the ash rejection and increases flotation recovery for coals of different rank with the exception of lign...

S S 100 Calcium - Binding Protein ▶ S 100 Proteins S 100 Proteins

S100 proteins were first discovered in 1965 by Moore as a major protein fraction (0.6% of total soluble protein) isolated from bovine brain (Moore 1965). The protein was given the name S100 due to its high solubility in saturated ammonium sulfate. Later experiments showed the S100 protein fraction constituted two different dimeric species comprised of two b protomers (S100B) or an a, b heterodi...

S 100 P ( S 100 calcium binding protein P )

S100P protein consists of 95 amino acids with a molecular weight of 10.4 kDa. S100P is a Ca binding protein that belongs to S100 family ("Soluble in 100% saturated solution with ammonium sulfate") which was first isolated from human placenta and is therefore designated as "P". S100 family includes at least 26 members, which are thought to be expressed only in vertebrates and are present in a ti...

Regulation of S 100 A