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Volumn 42, Issue 3, 2000, Pages 97-103

Cryosolvents useful for protein and enzyme studies below -100°C

Author keywords

Cryoenzymology; Cryosolvent; DSC; Methanol; Phase change; X ray diffraction

Indexed keywords

ACETONE; ALCOHOL; ENZYME; ETHYLENE GLYCOL; GLYCEROL; M PROTEIN; METHANOL; N,N DIMETHYLFORMAMIDE; SOLVENT;

EID: 0342445403     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(99)00053-6     Document Type: Article
Times cited : (8)

References (9)
  • 1
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    • The use of subzero temperatures in biochemistry: Slow reactions
    • Douzou P. The use of subzero temperatures in biochemistry: slow reactions. Methods Biochem. Anal. 22:1974;401-512.
    • (1974) Methods Biochem. Anal. , vol.22 , pp. 401-512
    • Douzou, P.1
  • 2
    • 0000070465 scopus 로고
    • Physical chemical data for mixed solvents used in low temperature biochemistry
    • Fasman G.D. 3rd ed Ohio, USA: CRC Press
    • Douzou P., Hui-Bon-Hoa G., Maurel P., Travers F. Physical chemical data for mixed solvents used in low temperature biochemistry. Fasman G.D. 3rd ed Handbook of biochemistry and molecular biology. vol. 1:1976;520-539 CRC Press, Ohio, USA.
    • (1976) Handbook of Biochemistry and Molecular Biology , vol.1 , pp. 520-539
    • Douzou, P.1    Hui-Bon-Hoa, G.2    Maurel, P.3    Travers, F.4
  • 3
    • 0017340407 scopus 로고
    • Enzymology at subzero temperatures
    • Douzou P. Enzymology at subzero temperatures. Adv. Enzymol. 45:1977;157-272.
    • (1977) Adv. Enzymol. , vol.45 , pp. 157-272
    • Douzou, P.1
  • 4
    • 0018678581 scopus 로고
    • Cryocnzymology: The study of enzyme catalysis at subzero temperatures
    • Fink A.L., Geeves M.A. Cryocnzymology: The study of enzyme catalysis at subzero temperatures. Methods Enzymol. 63:1979;336-370.
    • (1979) Methods Enzymol. , vol.63 , pp. 336-370
    • Fink, A.L.1    Geeves, M.A.2
  • 5
    • 0028812131 scopus 로고
    • The effect of low temperatures on enzyme activity
    • More N., Daniel R.M., Petach H.H. The effect of low temperatures on enzyme activity. Biochem. J. 305:1995;17-20.
    • (1995) Biochem. J. , vol.305 , pp. 17-20
    • More, N.1    Daniel, R.M.2    Petach, H.H.3
  • 7
    • 0027431229 scopus 로고
    • Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1
    • Hudson R.C., Ruttersmith L.D., Daniel R.M. Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate AN1. Biochim. Biophys. Acta. 102:1993;244-250.
    • (1993) Biochim. Biophys. Acta , vol.102 , pp. 244-250
    • Hudson, R.C.1    Ruttersmith, L.D.2    Daniel, R.M.3
  • 8
    • 0023946361 scopus 로고
    • Stability and substrate specificity of a β-glucosidase from the thermophilic bacterium Tp8 cloned into E. coli
    • Plant A.R., Oliver J.E., Patchett M. L, Daniel R.M., Morgan H.W. Stability and substrate specificity of a β-glucosidase from the thermophilic bacterium Tp8 cloned into E. coli. Arch. Biochem. Biophys. 262:1988;181-188.
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 181-188
    • Plant, A.R.1    Oliver, J.E.2    Patchett, M.L.3    Daniel, R.M.4    Morgan, H.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.