Plasmin is an enzyme formed in the circulating blood, and many other extracellular fluids, from the zymogen plasminogen. Plasminogen is a single-chain glycoprotein with 790 amino acid residues. Activation to the active form, plasmin, by urokinase involves cleavage at the arg-val bond between residues 560 and 561, resulting in the formation of the 2-chain plasmin molecule held together by 2 disulfide linkages. The heavier chain contains about 411 residues and the lighter chain about 233. The main function of plasmin is the digestion of fibrin in blood clots. Plasmin is a proteolytic enzyme with a specificity similar to that of trypsin. Like trypsin, plasmin belongs to the family of serine proteinases, in which the active site catalytic triad, his-57, asp-102, and ser-195 (chymotrypsin numbering), is situated in the light chain.
Plasmin acts as a proteolytic factor in a variety of processes other than fibrinolysis; including embryonic development, tissue remodelling, tumour invasion and inflammation; in ovulation it weakens the walls of the Graafian follicle. A Deficiency of plasmin may lead to thrombosis, as clots are not degraded adequately.
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