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Characterization of the kinetic and regulatory properties of high affinity calcium atpase activity in acinar preparations of rat submandibular salivary glands


, : Characterization of the kinetic and regulatory properties of high affinity calcium atpase activity in acinar preparations of rat submandibular salivary glands. Archives of Oral Biology 30(8): 587-594

High-affinity Ca2+-ATPase activity was characterized in the total particulate fraction of acinar preparations from rat submandibular glands. The Ca2+ concentration (as Ca2+-ATP) at half of maximal activity was 82 .+-. 17 nM, the Hill coefficient was 2.36 .+-. 0.6 and activity reached a steady level at .apprx. 200 pmol Pi min-1 .mu.g of membrane protein-1 from 1 to 20 .mu.M Ca2+-ATP. High-affinity Ca2+-ATPase required micromolar concentrations of Mg2+ and was inhibited .apprx. 60 per cent by the phenothiazine derivative, fluphenazine, but was unaffected by ouabain, Na+, K+, La3+, ruthenium red, oligomycin and added calmodulin. Kinetics of adenosine diphosphate, guanosine triphosphate, uridine triphosphate and inosine triphosphate hydrolysis were similar to those of Ca2+-ATP but p-nitrophenylphosphate was a poor substrate. In the heavy microsomal fraction of whole glands, active Ca2+ uptake (ATP-dependent, oxalate-enhanced and abolished by A23187) was measurable in the absence of added Mg2+, was inhibited by fluphenazine and was stimulated by submicromolar concentrations of Ca2+-ATP. Thus, rat submandibular glands contain the enzymic basis of active Ca2+ transport and can actively transport Ca2+. Both activities are stimulated at Ca2+ concentrations typical of the cytosol, appear to be positively cooperative and may be regulated, in part, by calmodulin.

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