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- W2023264571 abstract "Abstract 1. 1. The partial purification of the soluble cholinesterase from Squilla mantis is described. 2. 2. Affi-Gel Blue chromatography has represented the most efficient step in the purification of the enzyme. 3. 3. A single form of cholinesterase is present in the soluble fraction (70,000 g supernatant) of Squilla mantis homogenate. The isoelectric point is 5.3. 4. 4. Although propionylthiocholine was hydrolyzed at a higher rate than other substrates, Vmax/Km values indicated substrates containing acetic acid (acetylthiocholine and acetyl-β-methylthiocholine) showed a better affinity for the enzyme. 5. 5. Tetramethyl-, tetraethyl-, tetrapropyl- and tetrabutyl-ammonium ions are all linear competitive inhibitors of the hydrolysis of acetyl- and propionylthiocholine. 6. 6. Some kinetic, structural and phylogenetic features of the enzyme are discussed." @default.
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- W2023264571 date "1988-01-01" @default.
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- W2023264571 title "Characterization of the soluble cholinesterase from Squilla mantis" @default.
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