Ficin is a cysteine proteinase isolated from the latex of a Ficus tree. Ficin is known as fig tree latex. The latex of some species of Ficus (Moraceae) has been traditionally used as vermifuge in Central and South America. It has been accepted that anthelmintic activity is due to the proteolytic fraction ficin.
Purification, characterization, and solvent-induced
thermal stabilization of ficin from Ficus carica.
J Agric Food Chem. 2008, Prakash V. Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Mysore, India.
Ficin is known to occur in multiple forms. Although crude ficin is of considerable commercial importance, ficin as such has not been fully characterized. A major ficin from the commercial crude proteinase mixture preparation of Ficus carica was purified and characterized.The enzyme was active in the pH range of 6.5-8.5, and maximum activity was observed at pH 7.0. The N-terminal core sequence of ficin has homology with N-terminal sequences of plant cysteine proteinases. The enzyme contains three disulfide bonds and a single free cysteine residue at the active site.
Anthelmintic activity of the latex of Ficus species.
J Ethnopharmacol. 1999. Instituto de Veterinária, Universidade Federal Rural do Rio de Janeiro, Brazil.
In the present study, the anthelmintic activity of the latex of Ficus insipida Willd. and Ficus carica L. was investigated in NIH mice naturally infected with Syphacia obvelata, Aspiculuris tetraptera and Vampirolepis nana. The latex of Ficus insipida, administered by intragastric route in doses of 4 ml/kg/day during three consecutive days, were effective in the removal of 38% of the total number of S. obvelata, being inexpressive in the removal of A. tetraptera (8%) and segments of V. nana (6%). The latex of F. carica, administered in doses of 3 ml/kg/day, during three consecutive days, was effective in the removal of S. obvelata (41%) and it did not produce significant elimination of A. tetraptera (2%) and V. nana (8%). The observed high acute toxicity with hemorrhagic enteritis, in addition to a weak anthelmintic efficacy, do not recommend the use of these lattices in traditional medicine.
Characterization of acid-induced molten globule like
state of ficin.
Int J Biol Macromol. 2009, Kumar PR, Prakash V. Department of Protein Chemistry and Technology, Central Food Technological Research Institute (A Constituent Laboratory of CSIR), Cheluvamba Mansion, KRS Road, Mysore, India.
Effect of pH on the conformational behaviour of ficin (EC 18.104.22.168), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about approximately 74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.
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