Cysteine proteases from the Asclepiadaceae plants latex exhibited thrombin and plasmin like activities

H. V. Shivaprasad, M. Riyaz, R. Venkatesh Kumar, K. K. Dharmappa, Shaista Tarannum, J. M. Siddesha, R. Rajesh, B. S. Vishwanath

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


In the present study we evaluated the presence of cysteine protease from the latex of four plants Asclepias curassavica L., Calotropis gigantea R.Br., Pergularia extensa R.Br. and Cynanchum puciflorum R.Br. belongs to the family Asclepiadaceae. Cysteine proteases from these plants latex exhibited both thrombin and plasmin like activities. Latex enzyme fraction in a concentration dependent manner induced the formation of clot in citrated blood plasma. Direct incubation of fibrinogen with latex enzyme fraction resulted in the formation of fibrin clot similar to thrombin enzyme. However prolonged incubation resulted in degradation of the formed fibrin clot suggesting plasmin like activity. Latex enzyme fraction preferentially hydrolyzed Aα and Bβ chains of fibrinogen to form fibrin clot. Latex enzyme fraction also hydrolyzed the subunits of fully cross linked fibrin efficiently, the order of hydrolysis was α-polymer > α-chains > β-chain and γ-γ dimer. Cysteine proteases from all the four Asclepiadaceae plants latex exhibited similar action on fibrinogen and fibrin. This study scientifically validate the use of plant latex in stop bleeding and wound healing by traditional healers all over the world.

Original languageEnglish (US)
Pages (from-to)304-308
Number of pages5
JournalJournal of Thrombosis and Thrombolysis
Issue number3
StatePublished - 2009


  • Asclepiadaceae
  • Cysteine proteases
  • Plasmin like enzymes
  • Thrombin like enzymes

ASJC Scopus subject areas

  • Hematology
  • Cardiology and Cardiovascular Medicine


Dive into the research topics of 'Cysteine proteases from the Asclepiadaceae plants latex exhibited thrombin and plasmin like activities'. Together they form a unique fingerprint.

Cite this