메뉴 건너뛰기




Volumn 134, Issue 4, 1999, Pages 631-636

Influence of hydrostatic pressure on L-glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus

Author keywords

[No Author keywords available]

Indexed keywords

CHAENOCEPHALUS ACERATUS;

EID: 0032861790     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002270050578     Document Type: Article
Times cited : (4)

References (30)
  • 1
    • 0031406893 scopus 로고    scopus 로고
    • Enzymes in Antarctic fish: Glucose-6-phosphate dehydrogenase and glutamate dehydrogenase
    • Ciardiello MA, Camardella L, Carratore V, di Prisco G (1997a) Enzymes in Antarctic fish: glucose-6-phosphate dehydrogenase and glutamate dehydrogenase. Comp Biochem Physiol 118A: 1031-1036
    • (1997) Comp Biochem Physiol , vol.118 A , pp. 1031-1036
    • Ciardiello, M.A.1    Camardella, L.2    Carratore, V.3    Di Prisco, G.4
  • 2
    • 0041195209 scopus 로고    scopus 로고
    • Enzymes of Antarctic fishes: Effect of temperature on catalysis
    • Ciardiello MA, Camardella L, di Prisco G (1997b) Enzymes of Antarctic fishes: effect of temperature on catalysis. Cybium 21: 443-450
    • (1997) Cybium , vol.21 , pp. 443-450
    • Ciardiello, M.A.1    Camardella, L.2    Di Prisco, G.3
  • 3
    • 0014198054 scopus 로고
    • Purification and kinetic characteristics of dogfish liver glutamate dehydrogenase
    • Corman L, Prescott LM, Kaplan NO (1967) Purification and kinetic characteristics of dogfish liver glutamate dehydrogenase. J biol Chem 242: 1383-1390
    • (1967) J Biol Chem , vol.242 , pp. 1383-1390
    • Corman, L.1    Prescott, L.M.2    Kaplan, N.O.3
  • 4
    • 0029971059 scopus 로고    scopus 로고
    • Hydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation
    • Dallet S, Legoy M-D (1996) Hydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation. Biochim biophys Acta 1294: 15-24
    • (1996) Biochim Biophys Acta , vol.1294 , pp. 15-24
    • Dallet, S.1    Legoy, M.-D.2
  • 5
    • 0345304096 scopus 로고    scopus 로고
    • Structure and function of hemoglobin and enzymes from antarctic organisms. The search for correlation with adaptive evolution
    • di Prisco G, Focardi S. Luporini P (eds) Camerino University Press, Camerino, Italy
    • di Prisco G, Camardella L, Carratore V, Ciardiello MA, Cocca E, D'Avino R, Romano M, Tamburrini M (1997) Structure and function of hemoglobin and enzymes from Antarctic organisms. The search for correlation with adaptive evolution. In: di Prisco G, Focardi S. Luporini P (eds) Proceedings of the 3rd meeting on Antarctic Biology. Camerino University Press, Camerino, Italy, pp 83-103
    • (1997) Proceedings of the 3rd Meeting on Antarctic Biology , pp. 83-103
    • Di Prisco, G.1    Camardella, L.2    Carratore, V.3    Ciardiello, M.A.4    Cocca, E.5    D'Avino, R.6    Romano, M.7    Tamburrini, M.8
  • 6
    • 4244084722 scopus 로고
    • Studies on the effect of ionic compounds on the stability of glutamate dehydrogenase
    • di Prisco G, Strecker HG (1966) Studies on the effect of ionic compounds on the stability of glutamate dehydrogenase. Biochim biophys Acta 122: 413-422
    • (1966) Biochim Biophys Acta , vol.122 , pp. 413-422
    • Di Prisco, G.1    Strecker, H.G.2
  • 7
    • 0028289989 scopus 로고
    • Stability and structural analysis of x-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23
    • Feller G, Payan F, Theys F, Qian M, Haser R, Gerday C (1994) Stability and structural analysis of x-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem 222: 441-447
    • (1994) Eur J Biochem , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.4    Haser, R.5    Gerday, C.6
  • 10
    • 0029924865 scopus 로고    scopus 로고
    • The pressure-dependence of two β-glucosidases with respect to their thermostability
    • Hamon V, Dallet S, Legoy M-D (1996) The pressure-dependence of two β-glucosidases with respect to their thermostability. Biochim biophys Acta 1294: 195-203
    • (1996) Biochim Biophys Acta , vol.1294 , pp. 195-203
    • Hamon, V.1    Dallet, S.2    Legoy, M.-D.3
  • 12
    • 0025303523 scopus 로고
    • A reactor permitting injection and sampling for steady state studies of enzymatic reactions at high pressure: Tests with aspartate transcarbamylase
    • Hui Bon Hoa G, Hamel G, Else A, Weill G, Hervé G (1990) A reactor permitting injection and sampling for steady state studies of enzymatic reactions at high pressure: tests with aspartate transcarbamylase. Analyt Biochem 187: 258-261
    • (1990) Analyt Biochem , vol.187 , pp. 258-261
    • Hui Bon Hoa, G.1    Hamel, G.2    Else, A.3    Weill, G.4    Hervé, G.5
  • 13
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R (1991) Protein stability and molecular adaptation to extreme conditions. Eur J Biochem 202: 715-728
    • (1991) Eur J Biochem , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 14
    • 0020484367 scopus 로고
    • The pressure-induced, reversible inactivation of mouse brain enolases
    • Kornblatt J, Kornblatt J, Hui Bon Hoa G (1982) The pressure-induced, reversible inactivation of mouse brain enolases. Eur J Biochem 128: 577-581
    • (1982) Eur J Biochem , vol.128 , pp. 577-581
    • Kornblatt, J.1    Kornblatt, J.2    Hui Bon Hoa, G.3
  • 15
    • 0009467932 scopus 로고
    • Activation volumes in enzymic catalysis: Their sources and modification by low-molecular-weight solutes
    • Low PS, Somero GN (1975) Activation volumes in enzymic catalysis: their sources and modification by low-molecular-weight solutes. Proc natn Acad Sci USA 72: 3014-3018
    • (1975) Proc Natn Acad Sci USA , vol.72 , pp. 3014-3018
    • Low, P.S.1    Somero, G.N.2
  • 16
    • 0023007922 scopus 로고
    • Thermodynamic arguments for temperature-induced cryptic conformational change of human plasma cholinesterase
    • Masson P, Balny C (1986) Thermodynamic arguments for temperature-induced cryptic conformational change of human plasma cholinesterase. Biochim biophys Acta 874: 90-98
    • (1986) Biochim Biophys Acta , vol.874 , pp. 90-98
    • Masson, P.1    Balny, C.2
  • 17
    • 0025202704 scopus 로고
    • Conformational plasticity of butyryl-cholinesterase as revelated by high pressure experiments
    • Masson P, Balny C (1990) Conformational plasticity of butyryl-cholinesterase as revelated by high pressure experiments. Biochim biophys Acta 1041: 223-231
    • (1990) Biochim Biophys Acta , vol.1041 , pp. 223-231
    • Masson, P.1    Balny, C.2
  • 18
    • 0029832690 scopus 로고    scopus 로고
    • Pressure effects on enzyme activity and stability at high temperatures
    • Michels PC, Hei D, Clark DS (1996) Pressure effects on enzyme activity and stability at high temperatures. Adv Protein Chem 48: 341-376
    • (1996) Adv Protein Chem , vol.48 , pp. 341-376
    • Michels, P.C.1    Hei, D.2    Clark, D.S.3
  • 20
    • 0018991620 scopus 로고
    • Denaturation and renaturation of bovine liver glutamic dehydrogenase after dissociation in various denaturants
    • Müller K, Jaenicke R (1980) Denaturation and renaturation of bovine liver glutamic dehydrogenase after dissociation in various denaturants. Z Naturf 35C: 222-228
    • (1980) Z Naturf , vol.35 C , pp. 222-228
    • Müller, K.1    Jaenicke, R.2
  • 21
    • 0019825281 scopus 로고
    • Pressure-dependent deactivation and reactivation of dimeric enzymes
    • Müller K, Lüdemann H-D, Jaenicke R (1981) Pressure-dependent deactivation and reactivation of dimeric enzymes. Naturwissenschaften 68: 524-525
    • (1981) Naturwissenschaften , vol.68 , pp. 524-525
    • Müller, K.1    Lüdemann, H.-D.2    Jaenicke, R.3
  • 22
    • 0028146899 scopus 로고
    • The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcux abyssi, a new deep-sea hyperthermophilic archaeobacterium
    • Purcarea C, Erauso G, Prieur D, Hervé G (1994) The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcux abyssi, a new deep-sea hyperthermophilic archaeobacterium. Microbiology 140: 1967-1975
    • (1994) Microbiology , vol.140 , pp. 1967-1975
    • Purcarea, C.1    Erauso, G.2    Prieur, D.3    Hervé, G.4
  • 23
    • 0029965266 scopus 로고    scopus 로고
    • Purification and characterization of carbamoyl-phosphate synthetase from the deep-sea hyperthermophilic archaebacterium Pyrococcus abyssi
    • Purcarea C, Simon V, Prieur D, Hervé G (1996) Purification and characterization of carbamoyl-phosphate synthetase from the deep-sea hyperthermophilic archaebacterium Pyrococcus abyssi. Eur J Biochem 236: 189-199
    • (1996) Eur J Biochem , vol.236 , pp. 189-199
    • Purcarea, C.1    Simon, V.2    Prieur, D.3    Hervé, G.4
  • 24
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva JL, Weber G (1993) Pressure stability of proteins. A Rev Phys Chem 44: 89-113
    • (1993) A Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2
  • 26
    • 0026583113 scopus 로고
    • Adaptations to high hydrostatic pressure
    • Somero GN (1992) Adaptations to high hydrostatic pressure. A Rev Physiol 54: 557-577
    • (1992) A Rev Physiol , vol.54 , pp. 557-577
    • Somero, G.N.1
  • 27
    • 0018543508 scopus 로고
    • Inefficient lactate dehydrogenase of deep-sea fishes
    • Somero GN, Siebenaller JF (1979) Inefficient lactate dehydrogenase of deep-sea fishes. Nature 282: 100-102
    • (1979) Nature , vol.282 , pp. 100-102
    • Somero, G.N.1    Siebenaller, J.F.2
  • 28
    • 0017187521 scopus 로고
    • Glutamate dehydrogenase from tuna liver. Purification, characteristics and sequence of a peptide containing an essential lysine residue
    • Veronese FM, Bevilacqua R, Boccù E, Brown DM (1976) Glutamate dehydrogenase from tuna liver. Purification, characteristics and sequence of a peptide containing an essential lysine residue. Biochim biophys Acta 445: 1-13
    • (1976) Biochim Biophys Acta , vol.445 , pp. 1-13
    • Veronese, F.M.1    Bevilacqua, R.2    Boccù, E.3    Brown, D.M.4
  • 30
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber G, Drickamer HG (1983) The effect of high pressure upon proteins and other biomolecules. Q Rev Biophys 16: 89-112
    • (1983) Q Rev Biophys , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.