1978
DOI: 10.1007/bf00689172
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Changes in the level of octopine during the escape responses of the scallop,Pecten maximus (L.)

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Cited by 75 publications
(28 citation statements)
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“…Argopecten irradians can use about 23-25 % of the glycogen stored in the adductor muscle, Epp et al 1988). Glycolysis leads to octopine formation, largely during recovery after swimming (Grieshaber and Gäde 1977;Gäde et al 1978;Chih and Ellington 1983); succinate formation may result from oxygen deficiency at mitochondrial level. In fact, P e O 2 remains low during recovery, such that scallops initially recover under hypoxic conditions, associated with a rise in P e CO 2 due to insufficient ventilation (MacDonald et al 2006).…”
Section: Mortalitymentioning
confidence: 99%
“…Argopecten irradians can use about 23-25 % of the glycogen stored in the adductor muscle, Epp et al 1988). Glycolysis leads to octopine formation, largely during recovery after swimming (Grieshaber and Gäde 1977;Gäde et al 1978;Chih and Ellington 1983); succinate formation may result from oxygen deficiency at mitochondrial level. In fact, P e O 2 remains low during recovery, such that scallops initially recover under hypoxic conditions, associated with a rise in P e CO 2 due to insufficient ventilation (MacDonald et al 2006).…”
Section: Mortalitymentioning
confidence: 99%
“…The OcDH-NADH-Larginine complex assembles with a K d of 5.5mmoll -1 during an enthalpically as well as a small entropically favoured reaction (Table1). The concentration of L-arginine, which according to Gäde et al (Gäde et al, 1978) ranges from 24 to 49mmoll -1 in resting and exhausted P. maximus, respectively, is more than sufficient for complex formation even in resting animals. [In order to understand how substrate changes might influence the binding behaviour to enzymes, substrate levels usually given in µmolg -1 wet mass must be converted to concentration in mmoll -1 (Chih and Ellington, 1986).…”
Section: D-octopine Binding and Dead-end Complex Formationmentioning
confidence: 99%
“…The small dissociation constants derived for NADH and D-octopine binding point to a relatively stable ternary complex, which is also likely to exist in vivo (Table1). Comparison of the kinetic data from inhibition studies of OcDH [inhibitor constant K i values range from 1.5 to 4mmoll -1 D-octopine Baldwin and Opie, 1978)] with in vivo substrate concentrations of D-octopine in exhausted or recovering scallops [9-15mmoll -1 (Baldwin and Opie, 1978;Gäde et al, 1978)] also support the proposal that the OcDH-NADH-D-octopine complex is formed in vivo at concentrations of ~12mmoll -1 D-octopine, exerting the known strong product inhibition of OcDH in exhausted scallops (de Zwaan et al, 1980;Chih and Ellington, 1986), D-octopine formation in the forward reaction appears to be substrate inhibited only to a small extent, if at all. Instead, OcDH can function as the terminal step of anaerobic glycolyis until Doctopine reaches concentrations in the range 10-15mmoll -1 during recovery.…”
Section: Substrate and Product Binding To Ocdh Dead-end Complexesmentioning
confidence: 99%
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