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J. Biol. Chem., Vol. 269, Issue 42, 26178-26183, 10, 1994
H Hilfiker, D Guerini and E Carafoli
Full-length cDNAs for the three human plasma membrane Ca2+ pump isoforms 2
(PMCA2) differently spliced at the A site were constructed and transferred
to baculovirus. The corresponding proteins were expressed after infection
in Sf9 insect cells. The proteins were expressed at high levels and
retained the canonical properties of the plasma membrane Ca2+ pump. The
alternative splicing process failed to produce functional differences
detectable with the methods used. The Ca(2+)-dependent ATPase activity of
the PMCA2 pumps had a 5-10-fold higher affinity for calmodulin than the
PMCA4 pump expressed in the same system. Experiments on the formation of
the phosphoenzyme intermediate from ATP revealed that the PMCA2 pumps had
higher affinity for ATP than did the PMCA4 counterpart. The response of the
two pump types to activating acidic phospholipids was the same.
Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase. Functional properties of the enzyme and its splicing products
Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), Zurich.
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