PMID: 16615860Apr 18, 2006Paper

Studies on low molecular mass phytocystatins purified from Phaseolus mungo (Urd)

Biochemistry. Biokhimii︠a︡
S SharmaB Bano

Abstract

In the present study two phytocystatins (thiol protease inhibitors) have been isolated and purified to homogeneity from Phaseolus mungo by a simple two-step procedure using ammonium sulfate fractionation and gel filtration on Sephacryl-100 HR. The latter procedure yielded two peaks of the inhibitors (PMC I and PMC II). The pH optimum of both phytocystatins was pH 7.0; the temperature optima for PMC I and PMC II were 65 and 70 degrees C, respectively. The molecular masses of the purified phytocystatins were 19 and 17 kD, respectively, as determined by SDS-PAGE and mass spectrometry. Antibodies raised against the purified cystatins gave a single precipitin line in Ouchterlony double immunodiffusion. Kinetics of inhibition showed that PMC I and PMC II strongly inhibit papain and ficin but not trypsin and chymotrypsin. Binding stoichiometry of PMC I and PMC II with both papain and ficin was 1 : 2. The effect of urea on PMC I and PMC II was analyzed by fluorescence and circular dichroism spectroscopy. The CD results suggest an unfolding of PMC I and PMC II accompanying a decrease in the amount of extended (hydrated) coil structure and an increase in sheet-like structure. FTIR results show that PMC I is structurally similar to PMC II...Continue Reading

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Citations

Jul 11, 2006·Biochemistry. Biokhimii︠a︡·F RashidB Bano
Jan 11, 2016·Journal of Molecular Recognition : JMR·Azaj AhmedBilqees Bano
Nov 16, 2016·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Shumaila KhanBilqees Bano

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