Biochemical Journal · 1952 · 20 citations · 7 references
Life SciencesBiochemistryPharmacologyBiochemical PharmacologyChemical KineticsEnzymologyCholinergic PharmacologyEnzyme InhibitionEnzyme KineticsMichaelis-menten KineticsTime-dependent KineticsReaction Rate Constants
Research Article| September 01 1952 Studies on cholinesterase. 8. Determination of reaction velocity constants with a reversible inhibitor of pseudo-cholinesterase D. K. Myers D. K. Myers 1Pharmaco-therapeutic Laboratory of the University of Amsterdam, Amsterdam, Holland Search for other works by this author on: This Site PubMed Google Scholar Biochem J (1952) 52 (1): 46–53. https://doi.org/10.1042/bj0520046 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation D. K. Myers; Studies on cholinesterase. 8. Determination of reaction velocity constants with a reversible inhibitor of pseudo-cholinesterase. Biochem J 1 September 1952; 52 (1): 46–53. doi: https://doi.org/10.1042/bj0520046 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search This content is only available as a PDF. © 1952 CAMBRIDGE UNIVERSITY PRESS1952 Article PDF first page preview Close Modal You do not currently have access to this content.
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A Note on the Kinetics of Enzyme Action
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The turnover number of cholinesterase
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