J
John T. Penniston
Researcher at Russian Academy of Sciences
Publications - 5
Citations - 385
John T. Penniston is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: ATPase & Signal. The author has an hindex of 5, co-authored 5 publications receiving 381 citations.
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Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump
TL;DR: The primary structure of a region of the erythrocyte plasma membrane calcium pump which is phosphorylated by the cAMP-dependent protein kinase has been determined and the sequence is A-P-T-K-R-N-S-S(P)-P-P
Journal ArticleDOI
The amino acid sequence of the phosphorylation domain of the erythrocyte Ca2+ ATPase.
TL;DR: The amino acid sequence of a peptide isolated from a CNBr digest of the erythrocyte Ca2+ ATPase has been determined and contains a highly conserved phosphorylation site sequence common to all aspartyl-phosphate forming ion motive ATPases which have been sequenced so far.
Journal ArticleDOI
Two Ca2+-requiring p-nitrophenylphosphatase activities of the highly purified Ca2+-pumping adenosinetriphosphatase of human erythrocyte membranes, one requiring calmodulin and the other ATP.
Anil K. Verma,John T. Penniston +1 more
TL;DR: Data show the existence of two types of NPP sites on the enzyme, one at which NPP is hydrolyzed and the other at which it inhibits ATP hydrolysis.