A direct extraction procedure successfully isolated an actin-like protein from sea urchin eggs, demonstrating salt-induced polymerization.
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Establishes salt-induced polymerization of actin-like protein in sea urchin eggs; leaves open conservation in vertebrate systems.
A direct extraction procedure for isolation of an actin-like protein from fresh sea urchin eggs was tried. The actin-like protein was found in the 10,000g supernatant of the egg homogenate. The crude extract obtained from the egg homogenate was purified by ammonium sulfate fractionation and dialysis against an ATP-cysteine solution. The purified actin-like protein occurred as 2.8S globular protein units, which transformed into heavy components of 7–8S and 12–13S on addition of salts. This change was accompanied by a rise in viscosity.
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T. Miki‐Noumura (1969) studied this question.
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