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Updated: May 17, 2026
Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
Published on: June 2, 2023
Purification and characterization of a novel antithrombotic peptide from Scolopendra subspinipes mutilans
Yi Kong1, Shi-Long Huang, Yu Shao
1School of Life Science & Technology, China Pharmaceutical University, 24 Tong Jia Xiang, Nanjing 210009, PR China. yikong668@163.com
Ethnopharmacological Relevance:
The centipede has been prescribed for the treatment of cardiovascular diseases in Korea, China and other Far Eastern Asian countries for several hundred years.
Materials And Methods:
A novel antithrombotic peptide was isolated from Scolopendra subspinipes mutilans using a combination of ultrafiltration, Sephadex G-50 column, Source 15Q anion exchange column and RP-HPLC C18 column.
Results:
The molecular mass of the purified peptide is 346Da measured by Electrospray Ionization Mass Spectrometry (ESI-MS). The primary structure of the peptide is Ser-Gln-Leu (SQL) determined by Edman degradation. SQL potently prolonged the activated partial thromboplastin time (aPTT), and inhibited platelet aggregation.
Conclusions:
These results help to clarify the mechanism of the antithrombotic activity of the centipede for effective treatment of cardiovascular and cerebrovascular diseases.
