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. 1967 Oct;58(4):1664–1668. doi: 10.1073/pnas.58.4.1664

Effect of local pH changes caused by substrate hydrolysis on the activity of membrane-bound acetylcholinesterase.

H I Silman, A Karlin
PMCID: PMC223977  PMID: 5237894

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brzin M. The localization of acetylcholinesterase in axonal membranes of frog nerve fibers. Proc Natl Acad Sci U S A. 1966 Nov;56(5):1560–1563. doi: 10.1073/pnas.56.5.1560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DIXON M. The determination of enzyme inhibitor constants. Biochem J. 1953 Aug;55(1):170–171. doi: 10.1042/bj0550170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Goldman R., Silman H. I., Caplan S. R., Kedem O., Katchalski E. Papain membrane on a collodion matrix: preparation and enzymic behavior. Science. 1965 Nov 5;150(3697):758–760. doi: 10.1126/science.150.3697.758. [DOI] [PubMed] [Google Scholar]
  4. HESTRIN S. Acylation reactions mediated by purified acetylcholine esterase. Biochim Biophys Acta. 1950 Jan;4(1-3):310–321. doi: 10.1016/0006-3002(50)90037-0. [DOI] [PubMed] [Google Scholar]
  5. HOSKIN F. C. Stereospecificity in the reactions of acetylcholinesterase. Proc Soc Exp Biol Med. 1963 Jun;113:320–321. doi: 10.3181/00379727-113-28354. [DOI] [PubMed] [Google Scholar]
  6. Karlin A. Chemical distinctions between acetylcholinesterase and the acetylcholine receptor. Biochim Biophys Acta. 1967 Jul 11;139(2):358–362. doi: 10.1016/0005-2744(67)90039-3. [DOI] [PubMed] [Google Scholar]
  7. LAWLER H. C. Turnover time of acetylcholinesterase. J Biol Chem. 1961 Aug;236:2296–2301. [PubMed] [Google Scholar]
  8. Leuzinger W., Baker A. L. Acetylcholinesterase, I. Large-scale purification, homogeneity, and amino Acid analysis. Proc Natl Acad Sci U S A. 1967 Feb;57(2):446–451. doi: 10.1073/pnas.57.2.446. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MICHEL H. O., KROP S. The reaction of cholinesterase with diisopropyl fluorophosphate. J Biol Chem. 1951 May;190(1):119–125. [PubMed] [Google Scholar]
  10. Nachmansohn D. Chemical control of the permeability cycle in excitable membranes during electrical activity. Ann N Y Acad Sci. 1966 Jul 14;137(2):877–900. doi: 10.1111/j.1749-6632.1966.tb50207.x. [DOI] [PubMed] [Google Scholar]
  11. WILSON I. B., ALEXANDER J. Acetylcholinesterase: reversible inhibitors, substrate inhibition. J Biol Chem. 1962 Apr;237:1323–1326. [PubMed] [Google Scholar]
  12. WILSON I. B., HARRISON M. A. Turnover number of acetyl-cholinesterase. J Biol Chem. 1961 Aug;236:2292–2295. [PubMed] [Google Scholar]

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