Lipid-binding serum glycoprotein Lipid-binding serum glycoprotein In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins. Members of this family include: These proteins consist of N- and C-terminal domains, which share a similar two-layer alpha/beta structure, but show little sequence identity to each other. Bactericidal permeability-increasing protein (BPI) is a potent antimicrobial protein of 456 amino acids that binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria. BPI contains two domains that adopt the same structural fold, even though they have little sequence similarity.
Sweat gland cell are actually pinched off, and disintegrate later to excrete sweat. In both apocrine and eccrine sweat glands, the sweat is originally produced in the gland's coil, where it is isotonic with the blood plasma there. When the rate of sweating is low, salt is conserved and reabsorbed by the gland's duct; high sweat rates, on the other hand, lead to less salt reabsorption and allow more water to evaporate on the skin (via osmosis) to increase evaporative cooling. Secretion of sweat occurs when the myoepithelial cell cells surrounding the secretory glands contract. Eccrine sweat increases the rate of bacterial