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Volumn 125, Issue 4, 1996, Pages 707-713

Survival of the intertidal pulmonate Onchidium tumidium during short term and long term anoxic stress

Author keywords

[No Author keywords available]

Indexed keywords

ONCHIDIUM TUMIDIUM;

EID: 0029759640     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00349253     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0000002475 scopus 로고
    • D-Glucose. Determination with hexokinase and glucose-6-phosphate dehydrogenase
    • Bergmeyer HU, Gawehn K (eds) Academic Press, New York
    • Bergmeyer HU, Bernt E, Schmidt E, Stork H (1974) D-Glucose. Determination with hexokinase and glucose-6-phosphate dehydrogenase. In: Bergmeyer HU, Gawehn K (eds) Methods of enzymatic analysis. III. Academic Press, New York, pp 1196-1201
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1196-1201
    • Bergmeyer, H.U.1    Bernt, E.2    Schmidt, E.3    Stork, H.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding. Analyt Biochem 72: 248-259
    • (1976) Analyt Biochem , vol.72 , pp. 248-259
    • Bradford, M.M.1
  • 3
    • 0000926765 scopus 로고
    • Differential survival of Venus gallina and Scapharca inaequivalvis during anoxic stress: Covalent modification of phosphofructokinase and glycogen phosphorylase during anoxia
    • Brooks SPJ, de Zwaan A, Van den Thillart G, Cattani O, Cortesi P, Storey KB (1991) Differential survival of Venus gallina and Scapharca inaequivalvis during anoxic stress: covalent modification of phosphofructokinase and glycogen phosphorylase during anoxia J comp Physiol 161(B): 207-212
    • (1991) J Comp Physiol , vol.161 , Issue.B , pp. 207-212
    • Brooks, S.P.J.1    De Zwaan, A.2    Van Den Thillart, G.3    Cattani, O.4    Cortesi, P.5    Storey, K.B.6
  • 4
    • 0342435025 scopus 로고
    • Subcellullar enzyme binding in glycolytic control: In vivo studies with fish muscle
    • Brooks SPJ, Storey KB (1988) Subcellullar enzyme binding in glycolytic control: in vivo studies with fish muscle. Am J Physiol 225: R289-294
    • (1988) Am J Physiol , vol.225
    • Brooks, S.P.J.1    Storey, K.B.2
  • 5
    • 0025046194 scopus 로고
    • Glycolytic enzyme binding and metabolic control in estivation and anoxia in the land snail Otala lactea
    • Brooks SPJ, Storey KB (1990) Glycolytic enzyme binding and metabolic control in estivation and anoxia in the land snail Otala lactea. J exp Biol 151: 193-204
    • (1990) J Exp Biol , vol.151 , pp. 193-204
    • Brooks, S.P.J.1    Storey, K.B.2
  • 6
    • 0026064177 scopus 로고
    • Studies in the regulation of enzyme binding during anoxia in isolated tissues of Busycon canaliculatum
    • Brooks SPJ, Storey KB (1991a) Studies in the regulation of enzyme binding during anoxia in isolated tissues of Busycon canaliculatum. J exp Biol 156: 467-481
    • (1991) J Exp Biol , vol.156 , pp. 467-481
    • Brooks, S.P.J.1    Storey, K.B.2
  • 7
    • 0025957990 scopus 로고
    • Where is the glycolytic complex? A critical evaluation of the present data from muscle tissue
    • Brooks SPJ, Storey KB (1991b) Where is the glycolytic complex? A critical evaluation of the present data from muscle tissue. Fedn eur biochem Soc (FEBS) Lett 278(2): 135-138
    • (1991) Fedn Eur Biochem Soc (FEBS) Lett , vol.278 , Issue.2 , pp. 135-138
    • Brooks, S.P.J.1    Storey, K.B.2
  • 8
    • 0025894015 scopus 로고
    • A quantitative evaluation of the effect of enzyme complexes on the glycolytic rate in vivo: Mathematical modelling of the glycolytic complex
    • Brooks SPJ, Storey KB (1991c) A quantitative evaluation of the effect of enzyme complexes on the glycolytic rate in vivo: mathematical modelling of the glycolytic complex. J theor Biol 149: 361-375
    • (1991) J Theor Biol , vol.149 , pp. 361-375
    • Brooks, S.P.J.1    Storey, K.B.2
  • 9
    • 0000290117 scopus 로고
    • Intermediary energy metabolism during dormancy and anoxia in the land snail Otala lactea
    • Churchill TA, Storey KB (1989) Intermediary energy metabolism during dormancy and anoxia in the land snail Otala lactea. Physiol Zool 62(5): 1015-1030
    • (1989) Physiol Zool , vol.62 , Issue.5 , pp. 1015-1030
    • Churchill, T.A.1    Storey, K.B.2
  • 10
    • 9444271799 scopus 로고
    • Effect of electrical stimulation post mortem of bovine muscle on the binding of glycolytic enzymes
    • Clarke FM, Shaw FD, Morton DJ (1980) Effect of electrical stimulation post mortem of bovine muscle on the binding of glycolytic enzymes. Biochem J 136: 49-58
    • (1980) Biochem J , vol.136 , pp. 49-58
    • Clarke, F.M.1    Shaw, F.D.2    Morton, D.J.3
  • 11
    • 0001078829 scopus 로고
    • Energy metabolism during hypoxia in the isolated, perfused ventricle of the whelk, Busycon contrarium Condrad
    • Ellington WR (1981) Energy metabolism during hypoxia in the isolated, perfused ventricle of the whelk, Busycon contrarium Condrad. J comp Physiol 142(B): 457-464
    • (1981) J Comp Physiol , vol.142 , Issue.B , pp. 457-464
    • Ellington, W.R.1
  • 13
    • 0000831018 scopus 로고
    • L-(+)-Lactate. Determination with lactate dehydrogenase and NAD
    • Bergmeyer HU, Gawehn K (eds) Academic Press, New York
    • Gutmann I, Wahlefeld AW (1974) L-(+)-Lactate. Determination with lactate dehydrogenase and NAD. In: Bergmeyer HU, Gawehn K (eds) Methods of enzymatic analysis. III. Academic Press, New York, pp 1464-1472
    • (1974) Methods of Enzymatic Analysis. , vol.3 , pp. 1464-1472
    • Gutmann, I.1    Wahlefeld, A.W.2
  • 14
    • 0019309214 scopus 로고
    • Microcentrifuge desalting: A rapid, quantitative method for desalting small amounts of protein
    • Helmerhorst E, Stokes GB (1980) Microcentrifuge desalting: a rapid, quantitative method for desalting small amounts of protein. Analyt Biochem 104: 130-145
    • (1980) Analyt Biochem , vol.104 , pp. 130-145
    • Helmerhorst, E.1    Stokes, G.B.2
  • 16
    • 0343098594 scopus 로고
    • Limiting oxygen availability
    • Princeton University Press, Princeton, New Jersey
    • Hochachka PW, Somero GN (1985) Limiting oxygen availability. In: Biochemical adaptation. Princeton University Press, Princeton, New Jersey, pp 145-181
    • (1985) Biochemical Adaptation , pp. 145-181
    • Hochachka, P.W.1    Somero, G.N.2
  • 17
    • 0010244516 scopus 로고
    • Effects of anoxia on the activities of pyruvate kinase and phosphoenolpyruvate carboxykinase. and the production of lactate and succinate in the intertidal pulmonate Onchidium tumidium
    • Ip YK, Chew SF, Lee CY, Wong WP, Lim ALL, Murphy DL (1993) Effects of anoxia on the activities of pyruvate kinase and phosphoenolpyruvate carboxykinase. and the production of lactate and succinate in the intertidal pulmonate Onchidium tumidium. Mar Biol 116: 103-107
    • (1993) Mar Biol , vol.116 , pp. 103-107
    • Ip, Y.K.1    Chew, S.F.2    Lee, C.Y.3    Wong, W.P.4    Lim, A.L.L.5    Murphy, D.L.6
  • 20
    • 0002809955 scopus 로고
    • Effect of ischaemia on known substrates and cofactors on the glycolytic pathway in brain
    • Lowry OH, Panssonneau JV, Hasselberger FX, Schulz DW (1964) Effect of ischaemia on known substrates and cofactors on the glycolytic pathway in brain. J biol Chem 239: 18-30
    • (1964) J Biol Chem , vol.239 , pp. 18-30
    • Lowry, O.H.1    Panssonneau, J.V.2    Hasselberger, F.X.3    Schulz, D.W.4
  • 21
    • 0022973976 scopus 로고
    • The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin
    • Luther MA, Lee JC (1986) The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin. J biol Chem 261: 1753-1759
    • (1986) J Biol Chem , vol.261 , pp. 1753-1759
    • Luther, M.A.1    Lee, J.C.2
  • 22
    • 0026019041 scopus 로고
    • Evidence for phosphorylation/ dephosphorylation from organs of the anoxia tolerant sea mussel Mytilus edulis
    • Michaelidis B, Storey KB (1991) Evidence for phosphorylation/ dephosphorylation from organs of the anoxia tolerant sea mussel Mytilus edulis. J exp Zool 257: 1-9
    • (1991) J Exp Zool , vol.257 , pp. 1-9
    • Michaelidis, B.1    Storey, K.B.2
  • 23
    • 0000488594 scopus 로고
    • Glycolytic enzyme binding and metabolic control in anaerobiosis
    • Plaxton WC, Storey KB (1986) Glycolytic enzyme binding and metabolic control in anaerobiosis. J comp Physiol 156: 635-640
    • (1986) J Comp Physiol , vol.156 , pp. 635-640
    • Plaxton, W.C.1    Storey, K.B.2
  • 24
    • 0016372843 scopus 로고
    • Direct enzymatic procedure for the determination of liver glycogen
    • Roehrig KL, Allred JB (1974) Direct enzymatic procedure for the determination of liver glycogen. Analyt Biochem 58: 414-421
    • (1974) Analyt Biochem , vol.58 , pp. 414-421
    • Roehrig, K.L.1    Allred, J.B.2
  • 25
    • 0021731179 scopus 로고
    • Phosphofructokinase from foot muscle of the whelk, Busycotypus canaliculatum: Evidence for covalent modification of the enzyme during anaerobiosis
    • Storey KB (1984) Phosphofructokinase from foot muscle of the whelk, Busycotypus canaliculatum: evidence for covalent modification of the enzyme during anaerobiosis. Archs Biochem Biophys 235(2): 665-672
    • (1984) Archs Biochem Biophys , vol.235 , Issue.2 , pp. 665-672
    • Storey, K.B.1
  • 26
    • 0010456369 scopus 로고
    • A re-evaluation of the Pasteur effects: New mechanisms in anaerobic metabolism
    • Storey KB (1985a) A re-evaluation of the Pasteur effects: new mechanisms in anaerobic metabolism. Molec Physiol 8: 439-461
    • (1985) Molec Physiol , vol.8 , pp. 439-461
    • Storey, K.B.1
  • 27
    • 2142779586 scopus 로고
    • Fructose-2,6-bisphosphate and anaerobic metabolism in marine molluscs
    • Storey KB (1985b) Fructose-2,6-bisphosphate and anaerobic metabolism in marine molluscs. Fedn eur biochem Soc (FEBS) Lett 182(2): 245-248
    • (1985) Fedn Eur Biochem Soc (FEBS) Lett , vol.182 , Issue.2 , pp. 245-248
    • Storey, K.B.1
  • 28
    • 0000827866 scopus 로고
    • Adenosine-5′-triphosphate. UV-method with hexokinase and glucose-6-phosphate dehydrogenase
    • Bergmeyer J, Grassl M (eds) Academic Press, New York
    • Trautschold I, Lamprecht W, Schweitzer G (1985) Adenosine-5′-triphosphate. UV-method with hexokinase and glucose-6-phosphate dehydrogenase. In: Bergmeyer J, Grassl M (eds) Methods of enzymatic analysis. VII. Academic Press, New York, pp 346-357
    • (1985) Methods of Enzymatic Analysis , vol.7 , pp. 346-357
    • Trautschold, I.1    Lamprecht, W.2    Schweitzer, G.3
  • 29
    • 0000600144 scopus 로고
    • D-fructose-2,6-bisphosphate
    • Bergmeyer J, Grassl M (eds) Academic Press, New York
    • Van Schaftingen E (1984) D-fructose-2,6-bisphosphate. In: Bergmeyer J, Grassl M (eds) Methods of enzymatic analysis. VI. Academic Press, New York, pp 335-341
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 335-341
    • Van Schaftingen, E.1
  • 30
    • 0004173566 scopus 로고
    • Organ-specific regulation of phosphofructokinase during facultative anaerobiosis in the marine whelk, Busycotypus canaliculatum
    • Whitwam RE, Storey KB (1991) Organ-specific regulation of phosphofructokinase during facultative anaerobiosis in the marine whelk, Busycotypus canaliculatum. Can J Zool 69: 70-75
    • (1991) Can J Zool , vol.69 , pp. 70-75
    • Whitwam, R.E.1    Storey, K.B.2
  • 31
    • 0001657527 scopus 로고
    • L-Alanine. Determination with alanine dehydrogenase
    • Bergmeyer HU, Gawehn K (eds) Academic Press, New York
    • Williamson DH (1974) L-Alanine. Determination with alanine dehydrogenase. In: Bergmeyer HU, Gawehn K (eds) Methods of enzymatic analysis. IV. Academic Press, New York, pp 1679-1682
    • (1974) Methods of Enzymatic Analysis , vol.4 , pp. 1679-1682
    • Williamson, D.H.1
  • 32
    • 0001657527 scopus 로고
    • Succinate
    • Bergmeyer HU, Gawehn K (eds) Academic Press, New York
    • Williamson JR (1974) Succinate. In: Bergmeyer HU, Gawehn K (eds) Methods of enzymatic analysis. III. Academic Press, New York, pp 1616-1621
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1616-1621
    • Williamson, J.R.1


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