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A dimeric serine protease Neriifolin S of molecular mass 94kDa with milk clotting activity has been purified from the latex of Euphorbia neriifolia by anion exchange and size-exclusion chromatography. It hydrolyses peptidyl substrates l-Ala-pNA with highest affinity (K m of 0.195mM) and physiological efficiency (K cat /K m of 144.5mMs). Enzyme belongs to the class of neutral...
Neriifolin, a chymotrypsin-like serine protease, has been purified from the latex of Euphorbia neriifolia Linn. by ammonium sulfate precipitation, cation exchange chromatography and gel filtration. The molecular mass of the enzyme is 35.24kDa, with an isoelectric point of pH 5.7. The enzyme consists of 18 tryptophan, 25 tyrosine and 9 cysteine residues with 4 disulfide bridges. The extinction coefficient...
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