Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis.
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TLDR
In inside-out red cell membrane vesicles active calcium transport and the formation of the enzyme-phosphate complex (EP) of the calcium pump were simultaneously investigated and the effects of a limited proteolytic digestion examined, suggesting a probable molecular arrangement for the functional parts of the red cell membranes calcium pump.About:
This article is published in Journal of Biological Chemistry.The article was published on 1986-07-15 and is currently open access. It has received 146 citations till now. The article focuses on the topics: Calcium pump & Calcium.read more
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Journal ArticleDOI
Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases.
Gary E. Shull,J Greeb +1 more
TL;DR: A comparison of transport ATPases from diverse species has allowed the identification of a sequence that may form part of a second ATP binding site that suggests the possibility that additional diversity may occur via alternative processing of the primary transcript.
Journal ArticleDOI
Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain.
Éva Bakos,Raymond Evers,Gergely Szakács,Gábor E. Tusnády,Ervin Welker,Katalin Szabó,Marcel de Haas,Liesbeth van Deemter,Piet Borst,András Váradi,Balázs Sarkadi +10 more
TL;DR: Taken together, these experiments strongly suggest that the TMD0 region is neither required for the transport function of MRP1 nor for its proper routing to the plasma membrane.
Journal ArticleDOI
Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells
K. Maruyama,David H. MacLennan +1 more
TL;DR: The results demonstrate the absolute requirement of acylphosphate formation for the Ca2+ transport function and define a residue important for ATP binding and demonstrate the feasibility of a thorough analysis of active sites in theCa2+-ATPase by expression and site-specific mutagenesis.
Journal ArticleDOI
Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. A study using specific antibodies.
TL;DR: Antibodies against the four isoforms of the human plasma membrane Ca(2+)-ATPase (PMCA) were raised using an N-terminal sequence of the pump as epitope; in agreement with results in the rat, the protein was found in human neuronal tissues, particularly in the choroid plexus, but was practically absent in all other tissues tested.
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Cleavage of plasma membrane calcium pumps by caspases: a link between apoptosis and necrosis
B L Schwab,D Guerini,C Didszun,C Didszun,D Bano,Elisa Ferrando-May,Eugenio Fava,Eugenio Fava,John Tam,Daigen Xu,Steve Xanthoudakis,Donald W. Nicholson,Ernesto Carafoli,Pierluigi Nicotera,Pierluigi Nicotera +14 more
TL;DR: It is demonstrated that caspases cleave and inactivate the plasma membrane Ca2+ pump (PMCA) in neurons and non-neuronal cells undergoing apoptosis, and this event can lead to necrosis, an event that is reduced by caspase inhibitors in brain ischemia.
References
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Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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Transport adenosine triphosphatases: properties and functions
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The Ca2+-pumping ATPase of plasma membranes purification, reconstitution and properties
Ernesto Carafoli,Mauro Zurini +1 more
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The purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate.
TL;DR: Results suggest that the intermediate in the purified ATPase of the yeast Schizosaccharomyces pombe is an acylphosphate, and Plasma membranes contain several other minor phosphorylated components whose kinetic behavior is typical of phosphorylation by protein kinase.