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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Kallikrein-like enzyme from the venom of Agkistrodon p. piscivorus.

1. A kallikrein-like enzyme was isolated from Agkistrodon p. piscivorus venom by Sephadex G-100, DEAE-Sephacel and S-Sepharose column chromatographies. 2. A kallikrein-like enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodiffusion. 3. Its molecular weight is approx. 29,000 with an isoelectric point of 7. 8. 4. A kallikrein-like enzyme is able to cleave a kininogen analog to release bradykinin, and the B beta chain of fibrinogen. These proteolytic and tosyl-L-arginine methyl ester hydrolytic activities were inhibited by diisopropyl fluorophosphate, suggesting that the serine hydroxyl group is involved in enzymatic activities.[1]

References

  1. Kallikrein-like enzyme from the venom of Agkistrodon p. piscivorus. Nikai, T., Imai, K., Nagasaka, M., Sugihara, H. Int. J. Biochem. (1988) [Pubmed]
 
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