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Volumn 37, Issue 16, 1996, Pages 2691-2694

Is chorismate mutase a prototypic entropy trap? - Activation parameters for the Bacillus subtilis enzyme

Author keywords

[No Author keywords available]

Indexed keywords

CHORISMATE MUTASE;

EID: 0029928213     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/0040-4039(96)00338-3     Document Type: Article
Times cited : (113)

References (32)
  • 10
    • 85030197502 scopus 로고    scopus 로고
    • note
    • We noticed that chorismate mutase is easily released from E. coli cells when treated with high osmolarity buffer [20% (w/v) sucrose/30 mM Tris-HCl, pH 8.0/1 mM EDTA]. The highly enriched chorismate mutase fraction was chromatographed on DEAE DE-52 cellulose and then Sephadex G-75. A detailed protocol will be published elsewhere. Electrospray mass spectrometric analysis gave a subunit mass of 14487 ± 2 Da (calculated mass = 14489 Da). A prominent signal at 14357 Da (≈ 25% of 14487 peak) corresponds to a processed protein with cleaved N-terminal methionine. We believe that this truncation (seen in independent purifications and in samples from outside sources) occurs in vivo during protein synthesis and does not affect our results.
  • 12
    • 0023693095 scopus 로고
    • KA12 was constructed by generalized P1 transduction to delete the recA gene from strain KB224 (Balakrishnan, R.; Backman, K. Gene 1988, 67, 97-103.) according to a procedure described earlier: Kast, P.; Hennecke, H. J. Mol. Biol. 1991, 222, 99-124.
    • (1988) Gene , vol.67 , pp. 97-103
    • Balakrishnan, R.1    Backman, K.2
  • 13
    • 0026015417 scopus 로고
    • KA12 was constructed by generalized P1 transduction to delete the recA gene from strain KB224 (Balakrishnan, R.; Backman, K. Gene 1988, 67, 97-103.) according to a procedure described earlier: Kast, P.; Hennecke, H. J. Mol. Biol. 1991, 222, 99-124.
    • (1991) J. Mol. Biol. , vol.222 , pp. 99-124
    • Kast, P.1    Hennecke, H.2
  • 14
    • 0023087643 scopus 로고
    • 1H-NMR, analytical HPLC and, before each experiment, by quantitative conversion by chorismate mutase
    • 1H-NMR, analytical HPLC and, before each experiment, by quantitative conversion by chorismate mutase.
    • (1987) Methods Enzymol. , vol.142 , pp. 422-431
    • Connelly, J.A.1    Siehl, D.L.2
  • 15
    • 85030193494 scopus 로고    scopus 로고
    • note
    • Chorismate mutase concentration was determined using the Pierce BCA Protein Assay Reagent (Pierce, Rockford, IL) with bovine serum albumin as the calibration standard.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.