메뉴 건너뛰기




Volumn 139, Issue 1, 2001, Pages 113-126

Temperature effects on key metabolic enzymes in Littorina saxatilis and L. Obtusata from different latitudes and shore levels

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY; LATITUDE; MOLLUSC; TEMPERATURE EFFECT;

EID: 0034901852     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002270100557     Document Type: Article
Times cited : (74)

References (76)
  • 3
    • 0001702492 scopus 로고
    • Facultative anaerobiosis in Haliotis (ormer/abalone): Pyruvate kinase and phosphoenolpyruvate carboxy-kinase activities
    • (1984) Comp Biochem Physiol B , vol.77 , pp. 197-200
    • Bowen, C.E.1
  • 4
    • 0016414502 scopus 로고
    • Carbon dioxide utilisation and the regulation of respiratory metabolic pathways in parasitic helminths
    • Daves B (ed)
    • (1975) Adv Parasitol , vol.13 , pp. 35-69
    • Bryant, C.1
  • 8
    • 0001655244 scopus 로고
    • Anaerobic metabolism in sublittoral living Mytilus galloprovincialis Lam in the Mediterranean. II. Partial adaptation of pyruvate kinase and phosphoenolpyruvate carboxykinase
    • (1980) Comp Biochem Physiol B , vol.65 , pp. 513-518
    • De Vooys, C.G.N.1
  • 9
    • 0000790632 scopus 로고
    • Molluscs
    • Bryant C (ed) Metazoan life without oxygen. Chapman and Hall, London
    • (1991) , pp. 186-217
    • De Zwaan, A.1
  • 14
    • 0002431381 scopus 로고
    • Isocitrate dehydrogenase
    • Bergmeyer HU (ed) Methods of enzymatic analysis. VCH, Weinheim
    • (1987) , vol.3 , pp. 183-190
    • Goldberg, D.M.1    Ellis, G.2
  • 15
    • 0023010493 scopus 로고
    • A multilocus system for studying tissue and subcellular specialisation. The pH and temperature dependence of the two major NADP-dependent dehydrogenase isozymes of the fish Fundulus heteroclitus
    • (1986) J Biol Chem , vol.261 , pp. 11471-11477
    • Gonzalez-Villaseñor, L.I.1    Powers, D.A.2
  • 17
    • 0002130812 scopus 로고    scopus 로고
    • Temperature and growth rates as modulators of the metabolic capacities of fish muscle
    • Pörtner HO, Playle R (eds) Cold ocean physiology. Cambridge University Press, Cambridge
    • (1998) , pp. 58-87
    • Guderley, H.1
  • 26
    • 84971751548 scopus 로고
    • Differences in allele frequencies of AAT between high- and mid-rocky shore populations of Littorina saxatilis (Olivi) suggest selection in this enzyme locus
    • (1989) Genet Res , vol.54 , pp. 7-11
    • Johannesson, K.1    Johannesson, B.2
  • 36
    • 0016693127 scopus 로고
    • Pyruvate kinases and carbon dioxide fixating enzymes in the digestive gland of Littorina saxatilis rudis (Maton) and in the daughter sporocysts of Microphallus similis (Jaeg) (Digenea: Microphallidae)
    • (1975) Comp Biochem Physiol B , vol.51 , pp. 299-306
    • McManus, D.P.1    James, B.L.2
  • 38
    • 84971194589 scopus 로고
    • The behaviour of Littorina littorea (L) under natural conditions and its relation to position on the shore
    • (1958) J Mar Biol Assoc UK , vol.37 , pp. 229-239
    • Newell, G.E.1
  • 43
    • 0001505995 scopus 로고    scopus 로고
    • Levels of metabolic cold adaptation: Tradeoffs in eurythermal and stenothermal ectotherms
    • (in press) Davidson W, Williams HC (eds) Antarctic ecosystems: models for wider ecological understanding. Caxton Press, Christchurch, New Zealand
    • Pörtner, H.-O.1    Van Dijk, P.L.M.2    Hardewig, I.3    Sommer, A.4
  • 45
    • 0004374775 scopus 로고
    • Thermal inactivation of preparations of aspartic/glutamic transaminase from species of bivalved molluscs from the sublittoral and intertidal zones
    • (1963) Comp Biochem Physiol , vol.9 , pp. 161-180
    • Read, K.R.H.1
  • 48
    • 0001810816 scopus 로고
    • Aspartate aminotransferase (glutamate oxaloacetate transaminase)
    • Bergmeyer HU (ed) Methods of enzymatic analysis. VCH, Weinheim
    • (1987) , vol.3 , pp. 416-433
    • Rej, R.1    Horder, M.2
  • 50
    • 0023824296 scopus 로고
    • The role of stress proteins response in physiological adaptation of marine molluscs
    • (1988) Mar Environ Res , vol.24 , pp. 207-210
    • Sanders, B.M.1
  • 52
    • 77957219050 scopus 로고
    • Facultative anaerobiosis in the invertebrates: Pathways and control systems
    • (1971) Am Zool , vol.11 , pp. 125-135
    • Saz, H.J.1
  • 53
    • 0028339522 scopus 로고
    • Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenase operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria
    • (1994) FEBS Lett , vol.344 , pp. 109-116
    • Sazanov, L.A.1    Jackson, J.B.2
  • 62
    • 0016562591 scopus 로고
    • Temperature as a selective factor in protein evolution: The adaptational strategy of "compromise"
    • (1975) J Exp Zool , vol.194 , pp. 175-188
    • Somero, G.N.1
  • 63
    • 0002353040 scopus 로고
    • Temperature adaptation of enzymes: Biological optimisation through structure-function compromises
    • (1978) Annu Rev Ecol Syst , vol.9 , pp. 1-29
    • Somero, G.N.1
  • 65
    • 0002592440 scopus 로고    scopus 로고
    • Adaptation to cold and depth: Contrasts between polar and deep-sea animals
    • Pörtner HO, Playle RC (eds) Cold ocean physiology. Cambridge University Press, Cambridge
    • (1998) , pp. 33-57
    • Somero, G.N.1
  • 69
    • 0016527595 scopus 로고
    • Some embryogenic responses of mummichog, Fundulus heteroclitus (L) (Cyprinodontidae), to continuous incubation in various combinations of temperature and salinity
    • (1975) Can J Zool , vol.53 , pp. 920-933
    • Tay, K.L.1    Garside, E.T.2
  • 71
    • 0002916081 scopus 로고    scopus 로고
    • Kinetics of enzymes in coldstenothermal invertebrates
    • Pörtner HO, Playle RC (eds) Cold ocean physiology. Cambridge University Press, Cambridge
    • (1998) , pp. 190-211
    • Vetter, R.A.H.1    Buchholz, F.2
  • 72
    • 0001903439 scopus 로고
    • Respiratory metabolism and ecological characteristics of some fishes in McMurdo Sound, Antarctica
    • Lee MO (ed) Biology of the Antarctic seas
    • (1964) Antarct Res Ser , vol.1 , pp. 33-62
    • Wohlschlag, D.E.1
  • 75
    • 0018123414 scopus 로고
    • Properties of pyruvate kinase and phosphoenolpyruvate carboxykinase in relation to the direction and regulation of phosphoenolpyruvate metabolism in muscles of the frog and marine invertebrates
    • (1978) Biochem J , vol.174 , pp. 979-987
    • Zammit, V.A.1    Newsholme, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.