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PDB rendering based on 1b2i.
Available structures: 1b2i, 1bml, 1bui, 1cea, 1ceb, 1ddj, 1hpj, 1hpk, 1i5k, 1ki0, 1krn, 1l4d, 1l4z, 1pk4, 1pkr, 1pmk, 1qrz, 1rjx, 2doh, 2doi, 2pk4, 5hpg
Symbol(s) PLG; DKFZp779M0222
External IDs OMIM: 173350 MGI: 97620 Homologene: 55452
RNA expression pattern

More reference expression data

Human Mouse
Entrez 5340 18815
Ensembl ENSG00000122194 ENSMUSG00000059481
Uniprot P00747 Q3V1T9
Refseq NM_000301 (mRNA)
NP_000292 (protein)
NM_008877 (mRNA)
NP_032903 (protein)
Location Chr 6: 161.04 - 161.09 Mb Chr 17: 12.22 - 12.26 Mb
Pubmed search [1] [2]
Plasmin is an important enzyme (EC present in blood that degrades many blood plasma proteins, most notably fibrin clots. The degradation of fibrin is termed fibrinolysis.


It is a serine protease that is released as plasminogen into the circulation and activated by tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), thrombin, fibrin and factor XII (Hageman factor). It is inactived by alpha 2-antiplasmin, a serine protease inhibitor (serpin).

Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: it activates collagenases, some mediators of the complement system and weakens the wall of the Graafian follicle (leading to ovulation). It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor.


Deficiency in plasmin may lead to thrombosis, as clots are not degraded adequately.

Further reading

  • Anglés-Cano E, Rojas G (2003). "Apolipoprotein(a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site.". Biol. Chem. 383 (1): 93-9. PMID 11928826.
  • Ranson M, Andronicos NM (2004). "Plasminogen binding and cancer: promises and pitfalls.". Front. Biosci. 8: s294-304. PMID 12700073.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Plasmin". A list of authors is available in Wikipedia.
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