J. Biol. Chem., Vol. 261, Issue 19, 8601-8603, 07, 1986
Synthesis and characterization of a peptide segment of (Ca2+ + Mg2+)- ATPase. A candidate for calcium transport site
P Gangola and AE Shamoo
The second tryptic digestion (TD2) of the (Ca2+ + Mg2+)-ATPase results in
the decrease of Ca2+ transport due to uncoupling and the alteration of one
of the two high affinity sites to a low affinity site. The eight amino
acids adjacent to the tryptic digestion site form a torus with two
carboxylic side chains of one aspartic and one glutamic acid for the fast
twitch skeletal ATPase and two aspartic acids for the slow twitch/cardiac
ATPase toward the inside. The eight amino acid peptides were synthesized
for both forms of the ATPase and their binding characteristics were studied
with luminescent Eu3+ as a Ca2+ analogue. The data indicate that the
peptide binds Eu3+ with 1.0 Eu3+/peptide and strips off two water
molecules. The peptide region is a candidate for the Ca2+ transport site of
the (Ca2+ + Mg2+)-ATPase.
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