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A Caribbean copper plant peroxidase (CCPP) is purified from the latex of Euphorbia cotinifolia, using anion exchange chromatography. The molecular mass and isoelectic point of the enzyme is 43.11kDa and pH 8.1 respectively. The peroxidase is found to be sensitive towards general phenolic substrates like guaiacol, pyrogallol, α-aminopterin, phloroglucinol, o-phenelenediamine and dianisidine dihydrochloride...
A novel enzyme with endochitinase/lysozyme activity was purified to homogeneity from latex of Ipomoea carnea subsp. fistulosa using latex collection, gum removal, ammonium sulphate precipitation, hydrophobic interaction, and anion exchange chromatography. The enzyme was glycosylated (5–6%) and homogeneous on SDS-PAGE; has a molecular mass of 30.06kDa (MALDI-TOF) and an isoelectric point of pH 4.6...
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