Abstract
1. Actin-like protein (neurin) has been separated from actomyosin-like protein (neurostenin) isolated from bovine brain. This was accomplished by gel filtration chromatography (Sephadex G-200) and by ultracentrifugation in a continuous sucrose gradient containing 0.6 M KI. 2. The actin-like protein stimulated the Mg 2+-ATPase activity of muscle myosin. 3. It contained bound nucleotide which exchanged with free [ 14C]ATP. 4. It polymerized in the presence of 0.1 M KCl and 0.1 mM Mg 2+ with release of P i; increase in viscosity occurred upon dilution of the 0.6 M KI to 0.1 M. 5. The neurin reacted immunologically to form a single band with antiserum to neurostenin. 6. The neurin, similar to muscle actin, contained 3-methylhistidine. 7. The sedimentation constant of the protein was 2.8 S.
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