The carboxylesterases from Proteus vulgaris, Salmonella enterica and Citrobacter amalonaticus were purified 104-, 95- and 120-fold, respectively by chromatography. The enzymes had similar catalytic activities but differed considerably in their inactivation by heat, di-isopropyl fluorophosphate and Cd2+, Zn2+, Hg2+ and Cu2+. Quantitative neutralization of hydrolytic activity with specific immunoglobulins indicated that the three enzymes were antigenically distinct.
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Research progress in the extraction, purification, structural features, biological activities, and structure-activity relationships from Prunella vulgaris polysaccharides.
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Prunella vulgaris L., a globally recognized medicinal and edible plant, has been extensively used in China for over 2000 years, possessing the efficacy of clearing liver-fire, brightening the eyes, dispersing the knot, and reducing swelling. Phytochemical studies have shown that Prunella vulgaris contains various biologically active compounds, including flavonoids, triterpenes, polysaccharides, and phenolic acids.
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