Abstract
Being one of the most abundant proteins in human and other mammals, albumin plays a crucial role in transporting various endogenous and exogenous molecules and maintaining of colloid osmotic pressure of the blood. It is not only the passive but also the active participant of the pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities. A free thiol group of the albumin molecule determines the participation of the protein in redox reactions. Its activity is not limited to interaction with other molecules entering the blood: of great physiological importance is its interaction with the cells of blood, blood vessels and also outside the vascular bed. This entry contains data on the enzymatic, inflammatory and antioxidant properties of serum albumin.
Highlights
Physico-Chemical, Evolutionary and Genetic AspectsCitation: Belinskaia, D.A.; Voronina, P.A.; Batalova, A.A.; Goncharov, N.V
In addition to direct competition, the protein is susceptible to allosteric modulation: binding of a ligand in one site can affect the efficiency of binding in another
Due to the thiol group within Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species and participate in redox processes in the body
Summary
Albumin is a family of globular proteins, the most common of which are the serum albumins. Several other blood transport proteins are evolutionarily related to serum albumin, including alpha-fetoprotein, vitamin D-binding protein and afamin [2,3]. This family is only found in vertebrates [4]. The precursor of serum albumin (preproalbumin) has the N-terminal peptide, which is cut off before the protein leaves the rough endoplasmic reticulum. The product of this removal (proalbumin) is transported to the Golgi apparatus.
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