Large-scale purification and long-term stability of human butyrylcholinesterase: A potential bioscavenger drug

Journal of Biochemical and Biophysical Methods

Volumn 34, Issue 2, 1997, Pages 123-135

  Grunwald, Jacob ^a   Marcus, Dino ^a   Papier, Yoel ^a   Raveh, Lily ^a   Pittel, Zipora ^a   Ashani, Yacov ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

Author keywords

Human butyrylcholinesterase; Plasma; Procainamide gel; Purification; Stability

Indexed keywords

CHOLINESTERASE;

ANIMAL EXPERIMENT; ARTICLE; BIOAVAILABILITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STABILITY; GEL ELECTROPHORESIS; HUMAN; HUMAN TISSUE; INTRAVENOUS DRUG ADMINISTRATION; MALE; MOUSE; PLASMA; PRIORITY JOURNAL; STORAGE; TECHNIQUE; TEMPERATURE;

ANIMALS; BUTYRYLCHOLINESTERASE; ENZYME STABILITY; HUMANS; MICE; TEMPERATURE;

EID: 0030955779     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(97)01208-6     Document Type: Article

References (25)

1. Lockridge, O., Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine, Pharmacol. Ther., 47 (1990) 35-60.
2. Jbilo, O., Bartels, C.F., Chatonnet, A., Toutant, J.P. and Lockridge, O., Tissue distribution of human acetylcholinesterase and butyrylcholinesterase messenger RNA, Toxicon, 32 (1994) 1445-1457.
3. Schwarz, M., Glick, D., Lowenstein, Y. and Soreq. H., Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons, Pharm. Ther., 67 (1995) 283-322.
4. Viby-Mogensen, J., Succinylcholine neuromuscular blockade in subjects homozygous for atypical plasma cholinesterase, Anesthesiology, 55 (1981) 429-434.
5. Stewart, D.J., Inaba, T., Tang, B.K. and Kalow, W., Hydrolysis of cocaine in human plasma by cholinesterase, Life Sci., 20 (1977) 1557-1564.
6. Mattes, C., Bradley, R., Slaughter, E. and Browne, S., Cocaine and butyrylcholinesterase (BChE): Determination of enzymatic parameters, Life Sci., 58 (1996) 257-261.
7. Raveh, L., Grunwald, J., Marcus, D., Papier, Y., Cohen, E. and Ashani, Y., Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity: In vitro and in vivo quantitative characterization, Biochem. Pharmacol., 45 (1993) 2465-2474.
8. 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.
9. Kadar, T., Raveh, L., Brandeis, R., Grunwald, J., Cohen, E. and Ashani, Y. In D.M. Quinn, A.S. Balasubramanian, B.P. Doctor and P. Taylor, (Eds.), Enzymes of the Cholinesterase Family, Plenum Press, NY, 1995, pp. 404-405.
10. 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.
11. Porath, J. and Axen, R., Immobilization of enzymes to agar, agarose, and Sephadex supports, Methods Enzymol., 44 (1976) 19-45.
12. Lockridge, O. and La Du, B., Comparison of atypical and usual human serum cholinesterase, J. Biol. Chem., 253 (1978) 361-366.
13. Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227 (1970) 680-685.
14. Karnovsky, M.J. and Roots, L., A direct-coloring thiocholine method for cholinesterases, J. Histochem. Cytochem., 12 (1964) 219-221.
15. Ellman, G.L., Courtney, K.D., Andres, V., Jr. and Featherstone, R.M., A new and rapid colorimetric determination of acetylcholinesterase activity, Biochem. Pharmacol., 7 (1961) 88-95.
16. Lockridge, O., Eckerson, H.W. and LaDu, B.N., Interchain disulfide bonds and subunit organization in human serum cholinesterase, J. Biol. Chem., 254 (1979) 8324-8330.
17. Christian, S.T. and Beasley, J.G., Michaelis constants for isolated cholinesterase systems, J. Pharm. Sci., 57 (1968) 1025-1027.
18. Lockridge, O. and La Du, B.N., 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.
19. Levy, D. and Ashani, Y., Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase, Biochem. Pharmacol., 35 (1986) 1079-1085.
20. Brown, S.S., Kalow, W., Pilz, W., Whittaker, M. and Woronick, C.L., The plasma cholinesterases: A new perspective, Adv. Clin. Chem., 22 (1981) 1-123.
21. Masson, P., Adkins, S., Gouet, P. and Lockridge, O., Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant, J. Biol. Chem., 268 (1993) 14329-14341.
22. Delmar, E.G., Largman, C., Brodrick, J.W. and Geakas, M.C., A sensitive new substrate for chymotrypsin, Anal. Biochem., 99 (1979) 316-320.
23. Maxwell, D.M., The specificity of carboxylesterases protection against the toxicity of organophosphorus compounds, Toxicol. Appl. Pharmacol., 114 (1992) 306-312.
24. Gibaldi, M. and Perrier, D., Pharmacokinetics, Marcel Dekker, NY, 1982. pp. 410-417.
25. De La Hoz, D., Doctor, B.P., Ralston, J.C., Rush, R.S. and Wolfe, D.A., A simplified procedure for the purification of large quantities of fetal bovine serum acetylcholinesterase activity, Life Sci., 39 (1986) 195-199.