메뉴 건너뛰기




Volumn 187, Issue 1-3, 2010, Pages 23-26

How the cholinesterases got their modern names

Author keywords

Carbon analogues of choline esters; Dispersion forces; Enzyme substrate complementarity; Ion induced dipole interactions; True , pseudo , acetyl , butyryl cholinesterases

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE;

EID: 77955513812     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.02.041     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0001536516 scopus 로고
    • The action of certain esters and ethers of choline, and their relation to muscarine
    • Dale H.H. The action of certain esters and ethers of choline, and their relation to muscarine. J. Pharmacol. Exp. Ther. 1914, 6:147-190.
    • (1914) J. Pharmacol. Exp. Ther. , vol.6 , pp. 147-190
    • Dale, H.H.1
  • 2
    • 9644295236 scopus 로고
    • Pflügers Arch. Ges. Physiol. Über humoralen Übertragbarkeit der Herzenwirkung
    • Loewi O., Navratil E. Pflügers Arch. Ges. Physiol. Über humoralen Übertragbarkeit der Herzenwirkung. X. Über das Schicksal des Vagusstoffs 1926, 214:678-688.
    • (1926) X. Über das Schicksal des Vagusstoffs , vol.214 , pp. 678-688
    • Loewi, O.1    Navratil, E.2
  • 3
    • 0000162994 scopus 로고
    • Choline-esterase. An enzyme present in the blood serum of the horse
    • Stedman E., Stedman E., Easson L.H. Choline-esterase. An enzyme present in the blood serum of the horse. Biochem. J. 1932, 26:2056-2066.
    • (1932) Biochem. J. , vol.26 , pp. 2056-2066
    • Stedman, E.1    Stedman, E.2    Easson, L.H.3
  • 4
    • 0342768757 scopus 로고
    • Fermentative Azetylcholinspaltung im Blut und ihre Hemmung durch Physostigmin
    • Engelhart E., Loewi O. Fermentative Azetylcholinspaltung im Blut und ihre Hemmung durch Physostigmin. Naunyn-Schmiedebergs Arch. Exp. Path. Pharmakol. 1930, 150:1-13.
    • (1930) Naunyn-Schmiedebergs Arch. Exp. Path. Pharmakol. , vol.150 , pp. 1-13
    • Engelhart, E.1    Loewi, O.2
  • 5
    • 0006948286 scopus 로고
    • The action of blood on acetylcholine
    • Matthes K. The action of blood on acetylcholine. J. Physiol. 1930, 70:338-348.
    • (1930) J. Physiol. , vol.70 , pp. 338-348
    • Matthes, K.1
  • 6
    • 50249200408 scopus 로고
    • 1 deficiency: application of modern biochemical analysis in its diagnosis
    • 1 deficiency: application of modern biochemical analysis in its diagnosis. Lancet 1936, 227:1161-1164.
    • (1936) Lancet , vol.227 , pp. 1161-1164
    • Peters, R.A.1
  • 8
    • 0001488498 scopus 로고
    • Cholinesterases in the blood of man
    • Alles G.A., Hawes R.C. Cholinesterases in the blood of man. J. Biol. Chem. 1940, 133:375-390.
    • (1940) J. Biol. Chem. , vol.133 , pp. 375-390
    • Alles, G.A.1    Hawes, R.C.2
  • 9
    • 0343899610 scopus 로고
    • Studies on cholinesterase 3. Specific tests for true cholinesterase and pseudocholinesterase
    • Mendel B., Mundell D.B., Rudney H. Studies on cholinesterase 3. Specific tests for true cholinesterase and pseudocholinesterase. Biochem. J. 1943, 37:473-476.
    • (1943) Biochem. J. , vol.37 , pp. 473-476
    • Mendel, B.1    Mundell, D.B.2    Rudney, H.3
  • 11
    • 77955512827 scopus 로고
    • The specificity of the human erythrocyte cholinesterase
    • Adams D.H., Whittaker V.P. The specificity of the human erythrocyte cholinesterase. Biochem. J. 1948, 43:xiv-xv.
    • (1948) Biochem. J. , vol.43
    • Adams, D.H.1    Whittaker, V.P.2
  • 12
    • 4243638250 scopus 로고
    • The specificity of the human erythrocyte cholinesterase
    • Adams D.H. The specificity of the human erythrocyte cholinesterase. Biochim. Biophys. Acta 1949, 3:1-14.
    • (1949) Biochim. Biophys. Acta , vol.3 , pp. 1-14
    • Adams, D.H.1
  • 13
    • 77955510318 scopus 로고
    • The specificity of pigeon-brain cholinesterase
    • Whittaker V.P. The specificity of pigeon-brain cholinesterase. Biochem. J. 1949, 44:xlvi-xlvi10.
    • (1949) Biochem. J. , vol.44
    • Whittaker, V.P.1
  • 14
    • 0345204716 scopus 로고
    • The cholinesterases of human blood I. The specificity of the plasma enzyme and its relation to the erythrocyte cholinesterase
    • Adams D.H., Whittaker V.P. The cholinesterases of human blood I. The specificity of the plasma enzyme and its relation to the erythrocyte cholinesterase. Biochim. Biophys. Acta 1949, 3:358-366.
    • (1949) Biochim. Biophys. Acta , vol.3 , pp. 358-366
    • Adams, D.H.1    Whittaker, V.P.2
  • 15
    • 0011903293 scopus 로고
    • The cholinesterases of human blood II. The forces acting between enzyme and substrate
    • Adams D.H., Whittaker V.P. The cholinesterases of human blood II. The forces acting between enzyme and substrate. Biochim. Biophys. Acta 1950, 4:543-558.
    • (1950) Biochim. Biophys. Acta , vol.4 , pp. 543-558
    • Adams, D.H.1    Whittaker, V.P.2
  • 16
    • 76549243074 scopus 로고
    • The esterases of horse blood 1. The specificity of horse plasma cholinesterase and aliesterase
    • Sturge L.M., Whittaker V.P. The esterases of horse blood 1. The specificity of horse plasma cholinesterase and aliesterase. Biochem. J. 1950, 47:518-525.
    • (1950) Biochem. J. , vol.47 , pp. 518-525
    • Sturge, L.M.1    Whittaker, V.P.2
  • 17
    • 76549256371 scopus 로고
    • The esterases of horse blood 2. The specificity of horse erythrocyte cholinesterase
    • Mounter L.A., Whittaker V.P. The esterases of horse blood 2. The specificity of horse erythrocyte cholinesterase. Biochem. J. 1950, 47:525-530.
    • (1950) Biochem. J. , vol.47 , pp. 525-530
    • Mounter, L.A.1    Whittaker, V.P.2
  • 18
    • 0343629838 scopus 로고
    • The specificity of cobra-venom cholinesterase
    • Mounter L.A. The specificity of cobra-venom cholinesterase. Biochem. J. 1951, 50:122-128.
    • (1951) Biochem. J. , vol.50 , pp. 122-128
    • Mounter, L.A.1
  • 19
    • 0000736435 scopus 로고
    • Specificity, mode of action and distribution of cholinesterases
    • Whittaker V.P. Specificity, mode of action and distribution of cholinesterases. Physiol. Rev. 1951, 31:312-343.
    • (1951) Physiol. Rev. , vol.31 , pp. 312-343
    • Whittaker, V.P.1
  • 21
    • 76949114912 scopus 로고
    • The preparation of soluble cholinesterases from mammalian heart and brain
    • Ord M., Thompson R.H.S. The preparation of soluble cholinesterases from mammalian heart and brain. Biochem. J. 1951, 49:191-199.
    • (1951) Biochem. J. , vol.49 , pp. 191-199
    • Ord, M.1    Thompson, R.H.S.2
  • 22
    • 0022004427 scopus 로고
    • Pseudocholinesterase in Torpedo marmorata tissues: comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase
    • Toutant J.P., Massoulié J., Bon S. Pseudocholinesterase in Torpedo marmorata tissues: comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase. J. Neurochem. 1985, 44:580-592.
    • (1985) J. Neurochem. , vol.44 , pp. 580-592
    • Toutant, J.P.1    Massoulié, J.2    Bon, S.3
  • 23
    • 0001362811 scopus 로고
    • Acetylcholinesterase. VIII. Dissociation constants of the active groups
    • Wilson I.B., Bergmann F. Acetylcholinesterase. VIII. Dissociation constants of the active groups. J. Biol. Chem. 1950, 186:683-692.
    • (1950) J. Biol. Chem. , vol.186 , pp. 683-692
    • Wilson, I.B.1    Bergmann, F.2
  • 25
    • 50649087289 scopus 로고    scopus 로고
    • Acetylcholinesterase: how is its structure related to function?
    • Silman I., Sussman J.L. Acetylcholinesterase: how is its structure related to function?. Chem.-Biol. Interact. 2008, 175:3-10.
    • (2008) Chem.-Biol. Interact. , vol.175 , pp. 3-10
    • Silman, I.1    Sussman, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.