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Volumn 1435, Issue 1-2, 1999, Pages 177-183

A graphical method of analyzing pH dependence of enzyme activity

Author keywords

Dissociation constant; Enzyme activity; Hydrogen ion concentration; Linear plot; pH dependence

Indexed keywords

ENZYME;

EID: 0032752368     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00207-1     Document Type: Article
Times cited : (6)

References (10)
  • 1
    • 0001311360 scopus 로고
    • Principles of enzyme assay and kinetic studies
    • in: R. Eisenthal, M.J. Danson (Eds.) Oxford University Press, New York
    • K.F. Tipton, Principles of enzyme assay and kinetic studies, in: R. Eisenthal, M.J. Danson (Eds.), Enzyme Assays, Oxford University Press, New York, 1992, p. 48.
    • (1992) Enzyme Assays , pp. 48
    • Tipton, K.F.1
  • 4
    • 0000985115 scopus 로고
    • On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction
    • Alberty R.A., Massey V. On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction. Biochim. Biophys. Acta. 13:1954;347-353.
    • (1954) Biochim. Biophys. Acta , vol.13 , pp. 347-353
    • Alberty, R.A.1    Massey, V.2
  • 6
    • 0013556054 scopus 로고
    • Enzyme inhibition by excess substrate - exploitation of kinetic data, I. Linear method
    • Mamasse C. Enzyme inhibition by excess substrate - exploitation of kinetic data, I. Linear method. Biochim. Biophys. Acta. 77:1963;530-535.
    • (1963) Biochim. Biophys. Acta , vol.77 , pp. 530-535
    • Mamasse, C.1
  • 7
    • 0018721369 scopus 로고
    • Substrate inhibition
    • Cleland W.W. Substrate inhibition. Methods Enzymol. 63:1979;500-513.
    • (1979) Methods Enzymol. , vol.63 , pp. 500-513
    • Cleland, W.W.1
  • 8
    • 0031023550 scopus 로고    scopus 로고
    • Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068
    • Duffaud G.D., Mccutchen C.M., Leduc P., Parker K.N., Kelly R.M. Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068. Appl. Environ. Microbiol. 63:1997;169-177.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 169-177
    • Duffaud, G.D.1    McCutchen, C.M.2    Leduc, P.3    Parker, K.N.4    Kelly, R.M.5
  • 9
    • 0033531132 scopus 로고    scopus 로고
    • Prediction of photosynthetic production rate of ethylene using a recombinant cyanobacterium
    • Wang J.-S., Araki T., Ogawa T., Sakai M., Matsuoka M., Fukuda H. Prediction of photosynthetic production rate of ethylene using a recombinant cyanobacterium. J. Theor. Biol. 196:1999;9-17.
    • (1999) J. Theor. Biol. , vol.196 , pp. 9-17
    • Wang, J.-S.1    Araki, T.2    Ogawa, T.3    Sakai, M.4    Matsuoka, M.5    Fukuda, H.6
  • 10
    • 0000510324 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • in: R. Eisenthal, M.J. Danson (Eds.) Oxford University Press, New York
    • P.J.F. Henderson, Statistical analysis of enzyme kinetic data, in: R. Eisenthal, M.J. Danson (Eds.), Enzyme Assays, Oxford University Press, New York, 1992, p. 277.
    • (1992) Enzyme Assays , pp. 277
    • Henderson, P.J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.