Purification and characterization of a trypsin inhibitor from Putranjiva roxburghii seeds (original) (raw)

Purification and characterization of a trypsin inhibitor from Putranjiva roxburghii seeds

A highly stable and potent trypsin inhibitor was purified to homogeneity from the seeds of Putranjiva roxburghii belonging to Euphorbiaceae family by acid precipitation, cation-exchange and anion-exchange chromatography. SDS–PAGE analysis, under reducing condition, showed that protein consists of a single polypeptide chain with molecular mass of approximately 34kDa. The purified inhibitor inhibited bovine trypsin in 1:1 molar ratio. Kinetic studies