Solubility changes of proteins in sea urchin eggs upon fertilization.

The results presented in this paper give evidence of changes in solubility occurring in a protein fraction of the eggs of Arbacia lixula upon fertilization. The electrophoretic analysis indicates that it is only one part of one of the components of the KCl fraction that undergoes the change. However, under some experimental conditions (freezing and thawing of the KCl fraction or extraction of the whole eggs with water at room temperature) a larger portion of the KCl fraction, namely the whole group of components a and b, may be involved and undergoes coagulation. Therefore assuming that the results obtained on the extracts of frozen-dried fertilized eggs do reflect what actually occurs under natural conditions, we must also assume the existence of mechanisms controlling the extent of this change in the living eggs. The fact that in many cases one part or the whole of the sensitive fraction has been found to undergo an increase in solubility may suggest that the process of coagulation discovered by Mirsky is a two-step process. In the first step the sensitive fraction undergoes a change that makes it more soluble and then, when certain conditions are fulfilled, coagulation occurs. An alternative explanation could also be that the coagulated or coagulating fraction is attacked by the proteolytic enzyme that, as shown by Lundblad (1949, 1950), is activated on fertilization. This, however, seems to be less probable, as extraction was always carried out at 0 degrees C. and in as short a time as possible. However, further experiments are needed to decide whether the coagulation of the sensitive fraction is an actual occurrence under natural conditions. The results obtained with the eggs of Arbacia punctulata may cast some doubt on this assumption.