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Calcium dependent phosphatase and calcium dependent atpase activities in plasma membranes of eel anguilla rostrata gill epithelium 2. evidence for transport high affinity calcium atpase



Calcium dependent phosphatase and calcium dependent atpase activities in plasma membranes of eel anguilla rostrata gill epithelium 2. evidence for transport high affinity calcium atpase



Comparative Biochemistry and Physiology B 79(1): 9-16



Analysis of Ca2+-induced Mg .apprx. ATP-hydrolysis by eel gill plasma membranes revealed a substrate-specific, high-affinity Ca2+-ATPase activity (K0.5: 0.22 .mu.M, Vmax: 5.41 .+-. 0.63 .mu.mol Pi/h per mg protein) and a nonspecific, low-affinity phosphatase (K0.5 .gtoreq. 230 .mu.M, Vmax: 10.70 .+-. 1.25 .mu.mol Pi/h per mg protein). The high-affinity Ca2+-ATPase activity is calmodulin-dependent. The activation energy of the high-affinity Ca2+-ATPase, calculated on the basis of specific activities at 25 and 37.degree. C was 13.84 kcal mol. Specific activities of high-affinity Ca2+-ATPase and Na+/K+-ATPase were in the ratio of 1:20.4. The calmodulin-dependent, high-affinity Ca2+-ATPase shows characteristics of a transport Ca2+-ATPase; its association with Na+/K+-ATPase activity suggests that the branchial Ca2+-transport mechanism is concentrated in the chloride cells of the gills.

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