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Volumn 130, Issue 37, 2008, Pages 12456-12464

Direct site-selective covalent protein immobilization catalyzed by a phosphopantetheinyl transferase

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; BIOCHIPS; BIOSENSORS; CHEMICAL BONDS; CHEMICAL MODIFICATION; CLUSTERING ALGORITHMS; COLLOIDS; ENZYME ACTIVITY; ENZYMES; FOOD ADDITIVES; FUSION REACTIONS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MICROARRAYS; NUCLEAR PHYSICS; PROTEINS; RESINS; SYSTEM THEORY;

EID: 51949086070     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja8030278     Document Type: Article
Times cited : (97)

References (62)
  • 49
    • 51949103129 scopus 로고    scopus 로고
    • Luminescence assays of the resin after immobilization of ybbR-Luc from lysate demonstrated a significantly higher activity (410 au) compared to the controls with Sfp ommitted (36 au) and untreated resin (26 au, However, the luciferase activity resulting from the lysate was lower than the activity from the immobilization of purified ybbR-Luc Table 1, This is expected, given that the concentration of luciferase in the lysate was lower and endogenous CoA or acetyl-CoA present in the cell lysate can also compete as a substrate for the Sfp. In addition, ybbR-Luc is unstable at room temperature, and significant variations in specific activity of ybbR-Luc were observed between separately overproduced batches of the enzyme
    • Luminescence assays of the resin after immobilization of ybbR-Luc from lysate demonstrated a significantly higher activity (410 au) compared to the controls with Sfp ommitted (36 au) and untreated resin (26 au). However, the luciferase activity resulting from the lysate was lower than the activity from the immobilization of purified ybbR-Luc (Table 1). This is expected, given that the concentration of luciferase in the lysate was lower and endogenous CoA or acetyl-CoA present in the cell lysate can also compete as a substrate for the Sfp. In addition, ybbR-Luc is unstable at room temperature, and significant variations in specific activity of ybbR-Luc were observed between separately overproduced batches of the enzyme.
  • 54
    • 51949101014 scopus 로고
    • U.S. patent US5196306
    • (a) Bobrow, M. N.; Litt, G. J. U.S. patent US5196306, 1993.
    • (1993)
    • Bobrow, M.N.1    Litt, G.J.2
  • 59
    • 34249073784 scopus 로고    scopus 로고
    • Transglutaminase has been shown to catalyze protein immobilization: Tanaka, Y.; Tsuruda, Y.; Nishi, M.; Kamiya, N.; Goto, M. Org. Biomol. Chem. 2007, 5, 1764-1770. However, the selectivity and utility of this approach have yet to be fully established.
    • Transglutaminase has been shown to catalyze protein immobilization: Tanaka, Y.; Tsuruda, Y.; Nishi, M.; Kamiya, N.; Goto, M. Org. Biomol. Chem. 2007, 5, 1764-1770. However, the selectivity and utility of this approach have yet to be fully established.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.