Abstract
RECENT findings have indicated that serum cholinesterase of various mammals is not homogeneous, but that the hydrolytic activity is due to several isoenzymes1–4. Kinetic experiments5 as well as results obtained by Lawler6 suggest that cholinesterase is an aggregate of similar sub-units and it is conceivable that the enzyme may have various molecular weights according to the degree of aggregation. In order to pursue the problem further we have tried to separate the isoenzymes of cholinesterase by means of ultrafiltration. To prove the presence of different isoenzymes the kinetics of inhibition of the enzyme in the filtrate and supernatant has been studied by organophosphorus compounds.
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REINER, E., SEUFERTH, W. & HARDEGG, W. Occurrence of Cholinesterase Isoenzymes in Horse Serum. Nature 205, 1110–1111 (1965). https://doi.org/10.1038/2051110a0
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DOI: https://doi.org/10.1038/2051110a0
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