This paper discusses analytic techniques for understandingthe processes of Calcium-Dependent Atpase involving common eukaryotic enzyme.
Written in 1995; 2,925 words; 11 sources; $ 103.95
From the Paper:
"A common eukaryotic enzyme, calcium-dependent ATPase has been extensively investigated. The ion-transport enzyme uses energy derived from the hydrolysis of adenosine triphosphate (ATP) to move Ca2+ against a concentration gradient. Innumerable techniques have been applied to Ca2+-ATPase analyses. These have included proteolytic, genetic, immunologic, and molecular approaches.
Calcium-dependent ATPase was first isolated in 1970 (3:696-700). This heterogenous family of enzymes can be broadly subdivided into two separate groups. The plasma membrane Ca2+-ATPase occurs in most eukaryotic tissues. This 140-kDa enzyme binds calmodulin and is stimulated by calcium ion (10:285-297). Although it may be derived from plants, yeasts, or, for example,
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