Purification And Characterization Of A Protease From Ficus Hispida Linn
A sulphydryl plant protease obtained from the latex of Ficus hispida Linn was purified by chromatography on Sephadex g-200 upto 36-fold with a yield of 5.22% after initial purification by DEAE-cellulose chromatography. Molecular weight of the protease was estimated by Sephadex G-100 gel filtration and found to be around 23,700 daltons. The Michaelis constant (Km) with substrates haemoglobin and N-Î±-benzoyl-DL-arginine-p nitroanllide (BAPNA) was 1.25 mM and 0.83 mM, respectively. The activating and inhibiting effect of some chemical agents on the protease activity of the enzyme was also studied.