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Volumn 31, Issue 6, 1999, Pages 619-624

An emerging field in bioscience: High hydrostatic pressure study

Author keywords

Biological macromolecules; High hydrostatic pressure; Protein structure; Temperature effect; Thermodynamics

Indexed keywords


EID: 0342460739     PISSN: 05829879     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (15)
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    • Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and proteins complexes
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    • (1994) Eur J Biochem , vol.221 , pp. 617-630
    • Groß, M.1    Jaenicke, R.2
  • 4
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    • Exploiting the effects of high hydrostatic pressure in biotechnological applications
    • Mozhaev V, Heremans K, Frank J, Masson P, Balny C. Exploiting the effects of high hydrostatic pressure in biotechnological applications. TIBTECH, 1994, 12: 493-501
    • (1994) Tibtech , vol.12 , pp. 493-501
    • Mozhaev, V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 7
    • 0027762355 scopus 로고
    • Pressure stability of proteins
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    • (1993) Ann Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.1    Weber, G.2
  • 8
    • 0019327876 scopus 로고
    • Reversible high pressure dissociation of lactic dehydrogenase from pig muscle
    • Schade B C, Rudolph R, Lüdemann H D, Jaenicke R. Reversible high pressure dissociation of lactic dehydrogenase from pig muscle. Biochemistry, 1980, 19: 1121-1126
    • (1980) Biochemistry , vol.19 , pp. 1121-1126
    • Schade, B.C.1    Rudolph, R.2    Lüdemann, H.D.3    Jaenicke, R.4
  • 9
    • 0025265949 scopus 로고
    • Electrophoresis at elevated hydrostatic pressure of the multiheme hydroxylamine oxidoreductase
    • Masson P, Arciero D, Hooper A B, Balny C. Electrophoresis at elevated hydrostatic pressure of the multiheme hydroxylamine oxidoreductase. Electrophoresis, 1990, 11: 128-133
    • (1990) Electrophoresis , vol.11 , pp. 128-133
    • Masson, P.1    Arciero, D.2    Hooper, A.B.3    Balny, C.4
  • 10
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley S A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry, 1971, 10: 2436-2442
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 11
    • 0000357520 scopus 로고
    • Protein denaturation by high pressure. Measurements of turbidity of isoelectric ovalbumin and horse serum albumin under high pressure
    • Suzuki K, Miyosawa Y, Suzuki C. Protein denaturation by high pressure. Measurements of turbidity of isoelectric ovalbumin and horse serum albumin under high pressure. Arch Biochem Biophys, 1963, 101: 225-228
    • (1963) Arch Biochem Biophys , vol.101 , pp. 225-228
    • Suzuki, K.1    Miyosawa, Y.2    Suzuki, C.3
  • 12
    • 76549251971 scopus 로고
    • The influence of pressure on the rates of biological reactions
    • Laidler K J. The influence of pressure on the rates of biological reactions. Arch Biochem Biophys, 1950, 30: 226-236
    • (1950) Arch Biochem Biophys , vol.30 , pp. 226-236
    • Laidler, K.J.1
  • 13
    • 0019484519 scopus 로고
    • The theory of pressure effects on enzymes
    • Morild E. The theory of pressure effects on enzymes. Adv Prot Chem, 1981, 34: 93-166
    • (1981) Adv Prot Chem , vol.34 , pp. 93-166
    • Morild, E.1
  • 14
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    • Cryobaroenzymic studies as a tool for investigating activated complexes: Creatine kinase·ADP·Mg·nitrate·creatine as a model
    • Balny C, Travers F, Barman T, Douzou P. Cryobaroenzymic studies as a tool for investigating activated complexes: Creatine kinase·ADP·Mg·nitrate·creatine as a model. Proc Natl Acad Sci USA, 1985, 82: 7495-7499
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7495-7499
    • Balny, C.1    Travers, F.2    Barman, T.3    Douzou, P.4
  • 15
    • 0023275184 scopus 로고    scopus 로고
    • Thermodynamics of the two step formation of horseradish peroxidase compound I
    • Balny C, Travers F, Barman T, Douzou P. Thermodynamics of the two step formation of horseradish peroxidase compound I. Eur Biophys J, 1997, 14: 375-383
    • (1997) Eur Biophys J , vol.14 , pp. 375-383
    • Balny, C.1    Travers, F.2    Barman, T.3    Douzou, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.