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文献和实验Measurement of Ca2+-ATPase Activity (in PMCA and SERCA1)
and a purified enzyme, best suited for studies of Ca2+ -ATPase activity are described. The two selected membranes are the human red blood cell (RBC) ghosts, a representative of plasma membranes (PM), and the rabbit skeletal muscle SR, an intracellular membrane
Heterologous SERCA1a Ca2+ -ATPase (sarco-endoplasmic reticulum Ca2+ -adenosine triphosphatase isoform 1a) from rabbit was expressed in yeast Saccharomyces cerevisiae as a fusion protein, with a biotin acceptor domain (BAD) linked to the SERCA
Heterologous Expression of Human Membrane Receptors in the Yeast Saccharomyces cerevisiae
to those found in mammalian cells. The recombinant rabbit muscle Ca2+ -ATPase (adenosine triphosphatase), the first heterologously expressed mammalian MP for which the crystal structure was resolved, has been produced in S. cerevisiae . In this chapter, the focus
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