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Calretinin and calbindin in the retina of the developing chick
Calretinin and calbindin-D28k are two calcium-binding proteins that are present in largely different sets of nerve cells in the central nervous system, suggesting that these proteins may have distinct functions in differentiating cells.
Depression of calcium dynamics in cardiac myocytes--a common mechanism of halogenated hydrocarbon anesthetics and solvents.
The potency of the eight widely used HC to inhibit Ca2+ dynamics in cardiomyocytes correlated with their octanol/water partition coefficients and supported the hypothesis that alteration of Ca2- dynamics inCardiomyocyte is a common mechanism of cardiotoxic HC actions.
Occlusion of rubidium ions by the sodium‐potassium pump: its implications for the mechanism of potassium transport
1. The occlusion of rubidium ions by Na, K‐ATPase has been investigated by suspending enzyme prepared from pig kidney outer medulla in media containing low concentrations of 86Rb, forcing the
Calcium ion-dependent p-nitrophenyl phosphate phosphatase activity and calcium ion-dependent adenosine triphosphatase activity from human erythrocyte membranes.
The properties of the (ATP+Ca(2+))-dependent phosphatase are very similar to those of the Ca( 2+)-dependent ATPase (adenosine triphosphatase), also present in erythrocyte membranes, which probably is involved in Ca(2+) transport in ERYthrocytes.
Calcium binding by chick calretinin and rat calbindin D28k synthesised in bacteria.
Both calretinin and calbindin D28k bound 3-4 Ca2+/molecule, implying that at least one of the canonical EF-hand domains does not bind calcium.
Evidence for the ordered release of rubidium ions occluded within the Na,K‐ATPase of mammalian kidney.
It is shown that the free ions that prevent the rapid release of half of the Occluded rubidium themselves become occluded, compatible with the hypothesis that thefree rubidium or other ions act at the potassium‐loading sites at the extracellular face of the pump.