Lipid-binding proteins water soluble

Water-soluble compounds are naturally easily transported in the blood. Non-soluble compounds are usually transported bound to plasma proteins (albumins). This binding is reversible in most cases but may vary remarkably. The degree of protein binding may vary between 50% and 99%. The proportion of the free (unbound) compound in the circulation is the amount of the compound that can reach the tissues and thus the target organs. Very lipid-... 

Steroid and thyroid hormones are minimally soluble in the blood. Binding to plasma proteins renders them water soluble and facilitates their transport. Protein binding also prolongs the circulating half-life of these hormones. Because they are lipid soluble, they cross cell membranes easily. As the blood flows through the kidney, these hormones would enter cells or be... 

The remaining major classes of water-soluble lipid transporter proteins (other than the polyproteins of nematodes see below) come from plants and helminths. Plants possess very small (approximately 9 kDa) helix-rich, fatty-acid-binding proteins, the structures of some of which are known (Lerche and Poulsen, 1998). A recently described class comes from cestodes these are also very small (approximately 8 kDa), presumably intracellular, and helix-rich, and bind anthelmintic drugs in addition to fatty acids (Janssen and Barrett, 1995 Barrett et al., 1997). The only helix-rich small (approximately 14 kDa) lipid transporter from vertebrates is the acetyl-CoA-binding protein (Kragelund et al., 1993). 

If the virus is treated with proteolytic enzymes the fuzzy layer formed by the viral spikes is removed (Osterrieth, 1965 Compans, 1971 Gahm-berg et al, 1972 Sefton and Gaffney, 1974 Utermann and Simons, 1974). Remnants of both El and E2 are left in the bilayer. These have a hydrophobic amino acid composition, and are soluble in lipid solvents such as chloroform-methanol. The amphiphilic nature of the spike protein is also evident from its capacity to bind Triton X-100 (0.6 g/g protein) which binds to the hydrophobic part to form a water-soluble protein-detergent complex (Simons et al., 1973a). The ability of amphiphilic proteins to bind Triton can be used to separate them from hydrophilic proteins using an extraction procedure recendy described... 

The ability of a drug to penetrate cell membranes is determined by its chemical structure and its physicochemical properties, in particular the degree of ionisation, protein binding and lipid affinity. Lipid-soluble drugs diffuse easily across membranes, whereas water-soluble ones pass through at slower rates. 

Conjugation of lipophilic xenobiotics to polar cellular constituents renders the xenobiotic more water-soluble. While the lipophilic parent xenobiotics could readily diffuse into the cells, the increase in polarity associated with conjugation greatly reduces the ability of the compound to diffuse across the lipid bilayer of the cell membrane thus trapping the compound within the cell. The polar conjugates must therefore rely upon active transport processes to facilitate efflux from the cell. Hepatocytes, as well as other cells involved in chemical detoxification, are rich with members of the ATP-binding cassette superfamily of active transport proteins (ABC transporters). Cellular efflux of xenobiotics by these transporters is often referred to as Phase III elimination because Phase I or II detoxification processes often precede and are a requirement of Phase III elimination. A detailed description and discussion of elimination and transporters is presented in Chapter 15. 

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