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Volumn 48, Issue 2, 2010, Pages 347-362

New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase

Author keywords

Diphenolase activity; Kinetically preferred pathway; Monophenolase activity; Slow pathway; Tyrosinase

Indexed keywords


EID: 77954456405     PISSN: 02599791     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10910-010-9675-5     Document Type: Article
Times cited : (3)

References (27)
  • 1
    • 77954456647 scopus 로고    scopus 로고
    • A. Cornish-Bowden, in Fundamentals of enzyme kinetics, ed. by A. Cornish-Bowden (Butterworths, London, 1979), pp. 172-175.
  • 2
    • 77954458537 scopus 로고    scopus 로고
    • R. B. Silverman, in Contemporary enzyme kinetics and mechanism, ed. by D. L. Purich (San Diego, 2009), pp. 246-248.
  • 3
    • 77954458331 scopus 로고    scopus 로고
    • W. Ferdinand, in The enzyme molecule, ed. by W. Ferdinand (John Wiley and Sons, London, 1976), pp. 139-185.
  • 23
    • 77954457531 scopus 로고    scopus 로고
    • TM; Jandel Scientific: Core Madera (2006).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.