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The isolation of brain actomyosin‐like protein (neurostenin) with a Ca2+ ‐sensitive component is described. The addition of 1 mm EGTA results in approximately 50 per cent reduction in MgATPase activity. The inhibition can be released by a free Ca2+ concentration of 10−6m. Dialysis of the protein complex against low ionic strength medium followed by centrifugation results in a loss of Ca2+ sensitivity in the pelleted protein. Ca2+ sensitivity can be restored by reprecipitating this desensitized complex in the presence of the 70.000 g supernatant. The protection of sulphhydryl groups during desensitization and reconstitution procedures is essential. This Ca2+ regulatory property is similar, in these respects, to other actomyosin‐like proteins.
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Mahendran et al. (1974) studied this question.
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