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- W2017302540 abstract "In this paper, we have further analyzed the properties of calpain activator (CA) in order to better define its physiological function. The activator shows a pH optimum approximately 7.8–8.0, independently of the nature of the buffer used. Although the maximal activity is observed with human acid-denatured globin, the effect of CA is detectable with other protein substrates, such as casein and insulin. A comparable activating effect is observed also with the synthetic substrate Succ-Leu-Tyr-AMC. The activatory effect has been evaluated in a reconstructed system, using plasma membrane Ca2+-ATPase as substrate. CA is localized in erythrocyte precursor cells on the inner surface of the plasma membrane in very high amount and its level profoundly decreases up to 10% of the original value when cells reach the terminal differentiated state." @default.
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- W2017302540 date "2000-06-01" @default.
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- W2017302540 title "Properties and Intracellular Localization of Calpain Activator Protein" @default.
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- W2017302540 doi "https://doi.org/10.1006/bbrc.2000.2796" @default.
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