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. 1983 Feb 21;152(2):202-6.
doi: 10.1016/0014-5793(83)80380-9.

Purification of a troponin I-like factor from pig platelet

E der Terrossian, G Pruliere, A d'Albis
Free article

Purification of a troponin I-like factor from pig platelet

E der Terrossian et al. FEBS Lett. .
Free article

Abstract

A troponin I-like factor has been purified from pig platelet by G150 Sephadex filtration of a low ionic strength extract, acidification at pH 4.2, ion exchange on DE-52 cellulose, and affinity chromatography on calmodulin-Sepharose. This protein (Mr 17000), together with pig brain calmodulin and platelet tropomyosin, is able to participate to the reconstitution in vitro of a thin filament-like complex which modulates with 55% calcium sensitivity the platelet actin-activated Mg2+-dependent ATPase activity of rabbit skeletal muscle myosin.

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