FEBS Letters · 1994 · 44 citations · 37 references
We describe here an easy system for the production of mg amounts of the rabbit Ca(2+)-ATPase SERCA 1a in the yeast S. cerevisiae. The protein is present in several membranes, including the plasma membrane of the yeast, in a native conformation. It can be purified by immunoprecipitation and can be phosphorylated from ATP in a Ca(2+)-dependent manner. Using a temperature-sensitive secretion mutant strain, the fully active protein can also be obtained in secretory vesicles.
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Measurement of protein using bicinchoninic acid
Pam Smith, Randall I. Krohn, Greg T. Hermanson et al. · Analytical Biochemistry · 1985 · 18.2K citations