AMP-deaminase from sea scorpion white muscle: properties and redistribution under hypoxia

Lushchak, Volodymyr I.; Smirnova, Yulia D.; Storey, Kenneth B.

doi:10.1016/s0305-0491(98)00035-2

Cited by 16 publications

(25 citation statements)

References 20 publications

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“…At pH values of 5.5, 7.0 and 7.5, AMPD showed 56, 80 and 54% of its optimal activity, respectively. A similar, but sharper, pH dependency of AMPD activity was reported for the enzyme isolated from dog heart (Nechyporenko and Pohrebinska 1949) and sea scorpion white muscle (Lushchak et al 1998), whereas AMPD from trout heart and skeletal muscle had a similar pH dependency similar to that of the goldfish enzyme . However, the pH profile was found to depend on the concentration of the substrate .…”

Section: Resultssupporting

confidence: 64%

“…This is very different from the purified enzyme preparations from the muscle of trout (Lushchak and Storey 1994b), sea scorpion (Lushchak et al 1998) and elasmobranch fish (Makarewicz 1969), which were very unstable. However, this finding is in a good agreement with the data for carp AMPD (Purzycka-Preis and _ Zydowo 1969; Lushchak et al 2008).…”

Section: Resultsmentioning

confidence: 72%

“…This included AMPD from freshwater rainbow trout Oncorhynchus mykiss (Lushchak and Storey 1994a, b) and from marine fishes, such as the sea scorpion Scorpaena porcus and corb Sciaena umbra (Lushchak et al 1998). In contrast, Purzycka-Preis and _ Zydowo (1969) found that AMPD from common carp Cyprinus carpio muscle was rather stable, and these authors were able to partially characterize the enzyme.…”

Section: Introductionmentioning

confidence: 92%

“…In previous studies, we (Lushchak and Storey 1994a, b;Lushchak et al 1998) and others (Makarewicz 1969;Raffin 1983;Raffin 1984) have found that AMPD from fish muscle is not stable. This included AMPD from freshwater rainbow trout Oncorhynchus mykiss (Lushchak and Storey 1994a, b) and from marine fishes, such as the sea scorpion Scorpaena porcus and corb Sciaena umbra (Lushchak et al 1998).…”

Section: Introductionmentioning

confidence: 92%

“…intense exercise, hypoxia). The highest AMPD activity is generally found in skeletal muscle (Raffin et al 1993;Kaletha et al 1991;Lushchak and Storey 1994a, b;Lushchak et al 1998). Although there are many similarities between AMPD regulatory properties among vertebrate species, some specific features may differ.…”

Section: Introductionmentioning

confidence: 98%

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AMP-deaminase from goldfish white muscle: regulatory properties and redistribution under exposure to high environmental oxygen level

Lushchak

Husak

Storey

et al. 2008

Fish Physiol Biochem

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AMP-deaminase was partially purified from white skeletal muscle of goldfish, Carassius auratus. The enzyme was highly stable, showing virtually no change in activity at 1 month following the purification process when stored in 1 M KCl at 2-4 degrees C. The specific activity of the purified enzyme was 130-150 U/mg protein, with a pH optimum of about pH 6.5. AMP-aminohydrolase (AMPD) showed non-Michaelis-Menten kinetics, with a S(0.5) (half saturation by the substrate) for AMP of 0.73 +/- 0.03 mM, a Hill coefficient of 2.01 +/- 0.26, and a V(max) (maximum velocity) of 176 +/- 46 U/mg protein. Both sodium and potassium ions activated goldfish AMPD at low concentrations, with maximal activation at about 80 mM of each chloride salt, whereas higher concentrations became inhibitory. Magnesium and calcium ions also inhibited goldfish muscle AMPD, as did phosphate and fluoride; at a concentration of 8 mM, each anion reduced activity by about 66%. ADP and ATP were strong activators and both demonstrated concentration-dependent activation, with maximal effects at 0.5-1.5 mM. Fish exposure to a high concentration of oxygen (18-20 mg/l against 5-6 mg/l in the control) and recovery to the initial level induced a redistribution of AMPD between free and bound forms in goldfish white muscle and brain in a tissue-dependent manner. A spatial-temporal redistribution may be among the mechanisms regulating enzyme operation in vivo. Possible regulatory mechanisms of AMP-deaminase function in fish muscle are discussed.

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Section: Resultssupporting

confidence: 64%