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Volumn 5, Issue 12, 2009, Pages 1436-1445

Block-copolymer vesicles as nanoreactors for enzymatic reactions

Author keywords

Block copolymers; Enzymes; Fluorogenic substrates; Kinetics

Indexed keywords

BULK SOLUTIONS; CATALYTIC TURNOVER; CATALYZED REACTIONS; ENZYMATIC REACTION; FLUOROGENIC SUBSTRATE; FLUOROGENIC SUBSTRATES; INTERNAL VOLUME; LOADING EFFICIENCY; MICHAELIS-MENTEN CONSTANT; MONTE CARLO SIMULATION; NANO-SIZED REACTORS; NANOSCALE REACTORS; ORDERS OF MAGNITUDE; POLY(ACRYLIC ACID ); PREPARATION CONDITIONS; SMALL MOLECULES; SPATIAL CONFINEMENT; WALL COLLISION;

EID: 67650315430     PISSN: 16136810     EISSN: 16136829     Source Type: Journal    
DOI: 10.1002/smll.200801455     Document Type: Article
Times cited : (103)

References (30)
  • 2
    • 67650321273 scopus 로고    scopus 로고
    • 26th ed. (Eds.: R. K. Murray, D. K. Granner, P. A. Mayes, V. W. Rodwell ), Lange Medical Books/McGraw-Hill, New York
    • V. W. Rodwell, P. J. Kennelly, in Harper's Illustrated Biochemistry, 26th ed. (Eds.: R. K. Murray, D. K. Granner, P. A. Mayes, V. W. Rodwell ), Lange Medical Books/McGraw-Hill, New York 2003, pp. 49.
    • (2003) Harper's Illustrated Biochemistry , pp. 49
    • Rodwell, V.W.1    Kennelly, P.J.2
  • 22
    • 67650327304 scopus 로고    scopus 로고
    • [16] The cleavage of the peptide chains catalyzed by trypsin will liberate the fluorescent product R110, which will cause an increase in the emission intensity
    • Trypsin, a serine protease found in the digestive system, was used as the model enzyme. Trypsin predominantly cleaves peptide chains at the carboxyl side of lysine or arginine, which can be easily monitored by applying a fluorogenic substrate R110- Arg2.[16] The cleavage of the peptide chains catalyzed by trypsin will liberate the fluorescent product R110, which will cause an increase in the emission intensity.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.