Assesment of Na+/K+-ATPase, Mg2+-ATPase, Ca2+-ATPase, and Total-ATPase Activities in Gills of Freshwater Mussels Exposed to Penconazole
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Regulation of NaK-ATPase Activity by Neurotransmitters
The hitherto unknown NT-regulated mechanism of NaK-ATPase localized in the nerve ending membranes is found. The mechanism certainly has a functional significance and must be involved in the regulation – modulation of chemical synaptic transmission. On the other hand , the availability of the discovered specific protein, regulators (SFa and SFi) of synaptic origin, makes it possible to consider ...
متن کاملNa+-K+-ATPase and Na+/Ca2+ exchange activities in gills of hyperregulating Carcinus maenas.
Na+-K+-ATPase and Na+/Ca2+exchange activities were studied in gills of Carcinus maenas in seawater (SW) and after transfer to dilute seawater (DSW). Carcinushyperregulates its hemolymph osmolarity through active uptake of Na+, Cl-, and Ca2+. In DSW total Na+-K+-ATPase activity in posterior gills quadrupled; Na+/Ca2+ exchange specific activity was unaffected, and total activity increased 1.67-fo...
متن کاملComparative studies on the ATPase-binding sites in Ca2+-ATPase and (Na+ + K+)-ATPase by the use of ATP-analogues.
The effects of ATP-analogues on Ca2+-ATPase and (Na++ K+)-ATPase have been studied. The participation of sulfhydryl groups in the recognition of ATP by both transport ATPases is indicated by the fact, that the disulfide of thioinosine triphosphate inactivates both enzymes. The reactivity of rapidly and slowly reacting sulfhydryl groups in the ATP binding sites of both enzymes is altered by the ...
متن کاملimmunolocalization of na+,k+- atpase and ionocytes in gills of catfish,silurus glanis
introduction: the regulation of the body fluid content (osmoregulation) of an aquatic animal, is performed by several organs. in fish, osmoregulatory mechanisms are based on the function of specialized cells (ionocytes) located in various tissues and organs including gills. na+, k+-atpase is one of the main osmoregulatory enzymes enabling the use of atp as a source of energy for ion transport t...
متن کاملEffects of Mg2+, anions and cations on the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum.
In a previous paper [Gould, East, Froud, McWhirter, Stefanova & Lee (1986) Biochem. J. 237, 217-227] we presented a kinetic model for the activity of the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum. Here we extend the model to account for the effects on ATPase activity of Mg2+, cations and anions. We find that Mg2+ concentrations in the millimolar range inhibit ATPase activity, which...
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ژورنال
عنوان ژورنال: Commagene Journal of Biology
سال: 2019
ISSN: 2602-456X
DOI: 10.31594/commagene.632082