Abstract
Lactoylcholine is a choline ester which contains an asymmetric carbon atom in the acid portion of the molecule. A study of the hydrolytic rate of the enantiomers of this choline ester by human erythrocyte acetylcholinesterase revealed that the l(+) isomer is hydrolyzed at least four times greater than the d(−) isomer. The p S activity curve obtained for lactoylcholine assumed a typical acetylcholine-like bellshaped form. The p S optimum for l(+) isomer of lactoylcholine in comparison to acetylcholine shifted to a lower value, indicating a higher reaction velocity maximum at higher substrate concentrations. The differences in the relative enzymic rates of hydrolysis of the two isomers was explained by proposing the presence of an asymmetric reactive site on the enzyme surface facilitating the hydrolysis of one isomer better than the other.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
