Changes in the proteins of the sea urchin egg at fertilization

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Abstract

The sensitivity to trypsin and to heat denaturation of extracts of unfertilized and newly fertilized eggs of Arbacia lixula has been studied. The extracts have been also fractionated by precipitation at 50 per cent (fraction I) and 75 per cent (fraction II) saturation of ammonium sulphate and the fractions submitted to the same tests.

Extracts of fertilized eggs are more sensitive to trypsin than those of unfertilized eggs and the same is true for fraction II, whereas fraction I becomes slightly less sensitive after fertilization.

By the combined methods of the solubility in a salt buffer mixture and heat denaturation, it has been shown that upon fertilization the group of proteins of fraction I undergoes a decreased precipitability by the salt buffer at room temperature. The total amount of proteins precipitated by the salt-buffer after heating is also lower after fertilization. The significance of these results is discussed.

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The present investigations were supported by Grants of the Rockefeller Foundation and Consiglio Nazionale delle Ricerche.

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