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- W2078009093 abstract "Mild proteolysis by trypsin activates the purified (Ca2+ + Mg2+) - ATPase protein from human red cells in a way which is similar to the effect obtained by addition of calmodulin. The trypsin concentration required to reach half maximal effect in 3 minutes at 37°C is 2.5 – 3.5 μg/ml. SDS-poly-acrylamide gel electrophoresis reveals a degradation of the main protein (150'000 Dalton) into a large fragment (95'000 – 100'000 Dalton) and a small fragment (35'000 – 40'000 Dalton). Increasing ATPase activity correlates with the degree of proteolysis.The KCa of the digested (Ca2+ + Mg2+)-ATPase is 0.85 ± 0.1 μM Ca2+ as compared to 8.0 ± 0.75 μM Ca2+ before digestion and is statistically significantly different from KCa = 1.66 ± 0.22 μM Ca2+ observed in activation by a saturating calmodulin concentration. Addition of calmodulin to the trypsinized enzyme has neither an effect on the Ca2+-affinity nor achieves any large increase of the maximal rate.High Ca2+ concentrations (above 0.05 – 0.1 mM) after trypsin treatment still inhibit the (Ca2+ + Mg2+)-ATPase activity. Mg2+ activates in the same concentration range (KMg = 25 μM) as in the undigested preparation (KMg = 27 μM) and retains its competitive behaviour towards Ca2+ after trypsin treatment.It is concluded that (1) trypsin treatment unmasks high affinity sites for Ca2+ (KCa ∼ 1 μM) and that, therefore, such sites are not added to the system by calmodulin, and (2) that inhibition by high Ca2+-concentrations is not due to Ca - Mg competition at sites located on the calmodulin molecule." @default.
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- W2078009093 date "1981-12-01" @default.
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- W2078009093 title "Metal requirement of the isolated red cell Ca-pump ATPase after elimination of calmodulin dependence by trypsin attack" @default.
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- W2078009093 doi "https://doi.org/10.1016/0143-4160(81)90017-8" @default.
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