메뉴 건너뛰기




Volumn 61, Issue 2, 2008, Pages 191-196

Developing procedures for the large-scale purification of human serum butyrylcholinesterase

Author keywords

Butyrylcholinesterase; Cohn Fraction IV 4; Human plasma; Purification; Specific activity

Indexed keywords

CHOLINESTERASE; COHN FRACTION IV; DRUG DERIVATIVE; PLASMA PROTEIN; PROCAINAMIDE; SEPHAROSE;

EID: 50049116598     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.05.021     Document Type: Article
Times cited : (30)

References (33)
  • 1
    • 0024097963 scopus 로고
    • Structure of human serum cholinesterase
    • Lockridge O. Structure of human serum cholinesterase. Bioessays 9 (1988) 125-128
    • (1988) Bioessays , vol.9 , pp. 125-128
    • Lockridge, O.1
  • 4
    • 0031890563 scopus 로고    scopus 로고
    • Role of oligosaccharides in the pharmacokinetics of tissue-derived and genetically engineered cholinesterases
    • Saxena A., Ashani Y., Raveh L., Stevenson D., Patel T., and Doctor B.P. Role of oligosaccharides in the pharmacokinetics of tissue-derived and genetically engineered cholinesterases. Mol. Pharm. 53 (1998) 112-122
    • (1998) Mol. Pharm. , vol.53 , pp. 112-122
    • Saxena, A.1    Ashani, Y.2    Raveh, L.3    Stevenson, D.4    Patel, T.5    Doctor, B.P.6
  • 6
    • 0025962236 scopus 로고
    • Butyrylcholinesterase and acetylcholinesterase prophylaxis against soman poisoning in mice
    • Ashani Y., Shapira S., Levy D., Wolfe A.D., Doctor B.P., and Raveh L. Butyrylcholinesterase and acetylcholinesterase prophylaxis against soman poisoning in mice. Biochem. Pharmacol. 41 (1991) 37-41
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 37-41
    • Ashani, Y.1    Shapira, S.2    Levy, D.3    Wolfe, A.D.4    Doctor, B.P.5    Raveh, L.6
  • 8
    • 0027427279 scopus 로고
    • Prevention of soman-induced cognitive deficits by pretreatment with human butyrylcholinesterase in rats
    • Brandeis R., Raveh L., Grunwald J., Cohen E., and Ashani Y. Prevention of soman-induced cognitive deficits by pretreatment with human butyrylcholinesterase in rats. Pharmacol. Biochem. Behav. 46 (1993) 889-896
    • (1993) Pharmacol. Biochem. Behav. , vol.46 , pp. 889-896
    • Brandeis, R.1    Raveh, L.2    Grunwald, J.3    Cohen, E.4    Ashani, Y.5
  • 9
    • 0027241301 scopus 로고
    • Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity
    • Raveh L., Grunwald J., Marcus D., Papier Y., Cohen E., and Ashani Y. Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity. Biochem. Pharmacol. 45 (1993) 2465-2474
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 2465-2474
    • Raveh, L.1    Grunwald, J.2    Marcus, D.3    Papier, Y.4    Cohen, E.5    Ashani, Y.6
  • 10
    • 0031193319 scopus 로고    scopus 로고
    • The stoichiometry of protection against soman and VX toxicity in monkeys pretreated with human butyrylcholinesterase
    • Raveh L., Grauer E., Grunwald J., Cohen E., and Ashani Y. The stoichiometry of protection against soman and VX toxicity in monkeys pretreated with human butyrylcholinesterase. Toxicol. Appl. Pharmacol. 145 (1997) 43-53
    • (1997) Toxicol. Appl. Pharmacol. , vol.145 , pp. 43-53
    • Raveh, L.1    Grauer, E.2    Grunwald, J.3    Cohen, E.4    Ashani, Y.5
  • 11
    • 0033809639 scopus 로고    scopus 로고
    • Prospective of human butyrylcholinesterase as a detoxifying antidote and potential regulator of controlled-release drugs
    • Ashani Y. Prospective of human butyrylcholinesterase as a detoxifying antidote and potential regulator of controlled-release drugs. Drug Dev. Res. 50 (2000) 298-308
    • (2000) Drug Dev. Res. , vol.50 , pp. 298-308
    • Ashani, Y.1
  • 12
    • 0014221273 scopus 로고
    • Cholinesterase in plasma: first reported absence in the Bantu: half-life determination
    • Jenkins T., Balinsky D., and Patient D.W. Cholinesterase in plasma: first reported absence in the Bantu: half-life determination. Science 156 (1967) 1748-1750
    • (1967) Science , vol.156 , pp. 1748-1750
    • Jenkins, T.1    Balinsky, D.2    Patient, D.W.3
  • 14
    • 0024052137 scopus 로고
    • The use of serum cholinesterase in severe phosphorus poisoning. Personal experience
    • Cascio C., Comite C., Ghira M., Lanza G., and Ponchione A. The use of serum cholinesterase in severe phosphorus poisoning. Personal experience. Minerva Anesthesiol. 54 (1988) 337-338
    • (1988) Minerva Anesthesiol. , vol.54 , pp. 337-338
    • Cascio, C.1    Comite, C.2    Ghira, M.3    Lanza, G.4    Ponchione, A.5
  • 15
    • 0017153543 scopus 로고
    • Suxamethonium apnea terminated with commercial serum cholinesterase
    • Stovner J., and Stadskleiv K. Suxamethonium apnea terminated with commercial serum cholinesterase. Acta Anaesthesiol. Scand. 20 (1976) 211-215
    • (1976) Acta Anaesthesiol. Scand. , vol.20 , pp. 211-215
    • Stovner, J.1    Stadskleiv, K.2
  • 16
    • 0030007690 scopus 로고    scopus 로고
    • Administration of purified human plasma cholinesterase protects against cocaine toxicity in mice
    • Hoffman R.S., Morasco R., and Goldfrank L.R. Administration of purified human plasma cholinesterase protects against cocaine toxicity in mice. J. Toxicol. Ciln. Toxicol. 34 (1996) 259-266
    • (1996) J. Toxicol. Ciln. Toxicol. , vol.34 , pp. 259-266
    • Hoffman, R.S.1    Morasco, R.2    Goldfrank, L.R.3
  • 19
    • 0036070598 scopus 로고    scopus 로고
    • Wild-type and A328W mutant human butyrylcholinesterase tetramers expressed in Chinese hamster ovary cells have a 16-h half-life in the circulation and protect mice from cocaine toxicity
    • Duysen E.G., Bartels C.F., and Lockridge O. Wild-type and A328W mutant human butyrylcholinesterase tetramers expressed in Chinese hamster ovary cells have a 16-h half-life in the circulation and protect mice from cocaine toxicity. J. Pharmacol. Exp. Ther. 302 (2002) 751-758
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 751-758
    • Duysen, E.G.1    Bartels, C.F.2    Lockridge, O.3
  • 20
  • 21
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol. Ther. 47 (1990) 35-60
    • (1990) Pharmacol. Ther. , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 22
    • 0020581758 scopus 로고
    • Use of procainamide gels in the purification of human and horse serum cholinesterases
    • Ralston J.C., Main A.R., Kilpatrick B.F., and Chasson A.L. Use of procainamide gels in the purification of human and horse serum cholinesterases. Biochem. J. 211 (1983) 243-250
    • (1983) Biochem. J. , vol.211 , pp. 243-250
    • Ralston, J.C.1    Main, A.R.2    Kilpatrick, B.F.3    Chasson, A.L.4
  • 23
    • 0030955779 scopus 로고    scopus 로고
    • Large-scale purification and long-term stability of human butyrylcholinesterase: a potential bioscavenger drug
    • Grunwald J., Marcus D., Papier Y., Raveh L., Pittel Z., and Ashani Y. Large-scale purification and long-term stability of human butyrylcholinesterase: a potential bioscavenger drug. J. Biochem. Biophys. Methods 34 (1997) 123-135
    • (1997) J. Biochem. Biophys. Methods , vol.34 , pp. 123-135
    • Grunwald, J.1    Marcus, D.2    Papier, Y.3    Raveh, L.4    Pittel, Z.5    Ashani, Y.6
  • 24
    • 0022490455 scopus 로고
    • A simplified procedure for the purification of acetylcholinesterase from fetal bovine serum
    • De La Hoz D., Doctor B.P., Ralston J.S., Rush R.S., and Wolfe A.D. A simplified procedure for the purification of acetylcholinesterase from fetal bovine serum. Life Sci. 39 (1986) 195-199
    • (1986) Life Sci. , vol.39 , pp. 195-199
    • De La Hoz, D.1    Doctor, B.P.2    Ralston, J.S.3    Rush, R.S.4    Wolfe, A.D.5
  • 25
    • 0011112779 scopus 로고
    • Preparation and properties of serum and plasma proteins. Plasma cholinesterase
    • Surgenor D.M., and Ellis D. Preparation and properties of serum and plasma proteins. Plasma cholinesterase. J. Am. Chem. Soc. 76 (1954) 6049-6051
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 6049-6051
    • Surgenor, D.M.1    Ellis, D.2
  • 27
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidometric methods for measuring proteins
    • Layne E. Spectrophotometric and turbidometric methods for measuring proteins. Methods Enzymol. 3 (1957) 447-454
    • (1957) Methods Enzymol. , vol.3 , pp. 447-454
    • Layne, E.1
  • 28
    • 0017862859 scopus 로고
    • Comparison of atypical and usual human serum cholinesterase
    • Lockridge O., and La Du B. Comparison of atypical and usual human serum cholinesterase. J. Biol. Chem. 253 (1978) 361-366
    • (1978) J. Biol. Chem. , vol.253 , pp. 361-366
    • Lockridge, O.1    La Du, B.2
  • 29
    • 78651153462 scopus 로고
    • A direct-coloring thiocholine method for cholinesterases
    • Karnovsky M.J., and Roots L. A direct-coloring thiocholine method for cholinesterases. J. Histochem. Cytochem. 12 (1964) 219-221
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmeli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmeli, U.K.1
  • 31
    • 0029983402 scopus 로고    scopus 로고
    • Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters
    • Mattes C.E., Bradley R., Slaughter E., and Browne S. Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters. Life Sci. 58 (1996) 257-261
    • (1996) Life Sci. , vol.58 , pp. 257-261
    • Mattes, C.E.1    Bradley, R.2    Slaughter, E.3    Browne, S.4
  • 32
    • 0020491304 scopus 로고
    • Loss of interchain disulfide peptide and dissociation of the tetramer following limited proteolysis of native human serum cholinesterase
    • Lockridge O., and La Du B. Loss of interchain disulfide peptide and dissociation of the tetramer following limited proteolysis of native human serum cholinesterase. J. Biol. Chem. 257 (1982) 12012-12018
    • (1982) J. Biol. Chem. , vol.257 , pp. 12012-12018
    • Lockridge, O.1    La Du, B.2
  • 33
    • 27544478065 scopus 로고    scopus 로고
    • Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity
    • Lockridge O., Schopfer L.M., Winger G., and Woods J.H. Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity. J. Med. Chem. Biol. Radiol. Def. 3 (2005) 5095
    • (2005) J. Med. Chem. Biol. Radiol. Def. , vol.3 , pp. 5095
    • Lockridge, O.1    Schopfer, L.M.2    Winger, G.3    Woods, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.