Purification and reconstruction of the calcium, magnesium ATPase of the erythrocyte membrane.
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Biological Transport, Active↗
Biomedical subjects
V Niggli
Publications and source records attributed to V Niggli.
Calmodulin in natural and reconstituted calcium transporting systems.
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Animals↗
Purification of the (Ca2+-Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column.
The (Ca2+-Mg2+)-ATPase from human erythrocyte membranes has been solubilized in Triton X-100 and purified on a calmodulin affinity chromatography column in the presence of phosphatidylserine, to limit the inactivation of the enzyme. The enzyme was purified at least 150 times when compared with the original ghosts and showed a specific activity of 3.8 mumol.mg-1.min-1. In sodium dodecyl sulfate-polyacrylamide gels, a single major band was visible at a position corresponding to a molecular weight of about 125,000; a minor band (11% of the total protein) was present at a position corresponding to Mr = 205,000. Upon incubation of the purified preparation with [32P]ATP, both bands were phosphorylated in proportion to their mass, suggesting that both were active forms of purified ATPase.
Calcium-Transporting ATPases↗
Effects of calmodulin on the (Ca2+ + Mg2+)ATPase partially purified from erythrocyte membranes.
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Animals↗
Experiments on the mechanism of the inhibition of mitochondrial Ca2+ transport by La3+ and ruthenium red.
The effects of La3+ and ruthenium red on the energy-linked uptake of Ca2+ mediated by a synthetic neutral Ca2+ ionophore have been investigated in rat liver mitochondria. The results indicate that unspecific surface charge effects do not play a major role in the mechanism of inhibition of mitochondrial Ca2+ transport by La3+ and ruthenium red.
Animals↗
Characteristics of the active transport of Ca2+ by submitochondrial vesicles.
Inner membrane vesicles have been prepared by cholate treatment of rat liver mitoplasts. The vesicles can actively accumulate Ca2+ in the absence or presence of inorganic phosphate. The uptake is inhibited by ruthenium red and uncouplers of oxidative phosphorylation. Like in intact mitochondria the driving force for the uptake reaction seems to be the negative inside membrane potential generated during the oxidation of substrates. The level of antimycin-A-sensitive reduction of ferricyanide by succinate indicates that the cholate inner membrane vesicles are about 70% right side out. Using cytochrome-c-extracted inner membrane vesicles it can be shown that only those which have the same right-side-out polarity as intact mitochondria can actively accumulate Ca2+.
Animals↗