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 except the lips, ear canal, prepuce, glans penis, labia minora, and clitoris. They are ten times smaller than apocrine sweat glands, do not extend as deeply into the dermis, and excrete directly onto the surface of the skin. The proportion of eccrine glands decreases with age. The clear secretion produced by eccrine sweat glands is termed sweat or "sensible perspiration". Sweat is mostly water, but it does contain some electrolytes, since it is derived from blood plasma. The presence of sodium chloride gives sweat a salty taste. The total volume of sweat produced depends on the number of functional glands