메뉴 건너뛰기




Volumn 20, Issue 3, 2004, Pages 628-632

Sorting out molecules reacting with acetylcholinesterase by enzyme encapsulation in liposome

Author keywords

Encapsulation; Enzyme; Insecticides; Liposome; Selectivity

Indexed keywords

BIOSENSORS; CATALYSIS; HYDROPHOBICITY; IONIC STRENGTH; PH EFFECTS; SENSITIVITY ANALYSIS;

EID: 7444271974     PISSN: 09565663     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bios.2004.03.015     Document Type: Conference Paper
Times cited : (13)

References (10)
  • 1
    • 76549233982 scopus 로고
    • Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E605) and analogues
    • Aldridge W.N. Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E605) and analogues. Biochem. J. 46:1950;451-460
    • (1950) Biochem. J. , vol.46 , pp. 451-460
    • Aldridge, W.N.1
  • 2
    • 7444234449 scopus 로고    scopus 로고
    • Encapsulation of proteins in pre-formed liposomes
    • Chaize B., Winterhalter M., Fournier D. Encapsulation of proteins in pre-formed liposomes. Biotechniques. 34:2003;1-3
    • (2003) Biotechniques , vol.34 , pp. 1-3
    • Chaize, B.1    Winterhalter, M.2    Fournier, D.3
  • 3
    • 3042611512 scopus 로고    scopus 로고
    • Protein encapsulation in liposomes: Efficiency depends on interactions between proteins and phospholipid bilayer
    • Colletier, J.P., Chaize, B., Winterhalter, M., Fournier, D., 2002. Protein encapsulation in liposomes: efficiency depends on interactions between proteins and phospholipid bilayer. BMC Biotechnology, vol. 2, 2002.
    • (2002) BMC Biotechnology , vol.2 , pp. 2002
    • Colletier, J.P.1    Chaize, B.2    Winterhalter, M.3    Fournier, D.4
  • 5
    • 0036523648 scopus 로고    scopus 로고
    • Enzyme inhibition-based biosensors and biosensing systems: Questionable analytical devices
    • Luque de Castro M.D., Herrera M.C. Enzyme inhibition-based biosensors and biosensing systems: questionable analytical devices. Biosens. Bioelectron. 18:2003;279-294
    • (2003) Biosens. Bioelectron. , vol.18 , pp. 279-294
    • Luque De Castro, M.D.1    Herrera, M.C.2
  • 6
    • 0345542236 scopus 로고
    • Acceleration of the rate of reaction of dimetylcarbamyl and acetylcholinesterase by substituted ammonium ions
    • Metzger H.P., Wilson I.B. Acceleration of the rate of reaction of dimetylcarbamyl and acetylcholinesterase by substituted ammonium ions. J. Biol. Chem. 238:1963;3432-3435
    • (1963) J. Biol. Chem. , vol.238 , pp. 3432-3435
    • Metzger, H.P.1    Wilson, I.B.2
  • 7
    • 0035814370 scopus 로고    scopus 로고
    • Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation and protects against proteolytic degradation
    • Nasseau M., Boublik Y., Meier W., Winterhalter M., Fournier D. Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation and protects against proteolytic degradation. Biotechnol. Bioeng. 75:2001;615-618
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 615-618
    • Nasseau, M.1    Boublik, Y.2    Meier, W.3    Winterhalter, M.4    Fournier, D.5
  • 8
    • 0012512277 scopus 로고    scopus 로고
    • Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphates
    • Radic Z., Taylor P. Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphates. J. Appl. Toxicol. 21:2001;13-14
    • (2001) J. Appl. Toxicol. , vol.21 , pp. 13-14
    • Radic, Z.1    Taylor, P.2
  • 10
    • 0034826741 scopus 로고    scopus 로고
    • Enzymes inside lipid vesicles: Preparation, reactivity and applications
    • Walde P., Ichikawa A. Enzymes inside lipid vesicles: preparation, reactivity and applications. Biomol. Eng. 18:2001;143-177
    • (2001) Biomol. Eng. , vol.18 , pp. 143-177
    • Walde, P.1    Ichikawa, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.