Abstract
The properties of Urechis caupo microtubule protein in mature eggs was investigated and found to be similar to that of other organisms with respect to molecular weight and colchicine-binding parameters. Selective extraction from microtubule-rich organelles and vinblastine precipitation were used to identify and purify this protein, and two distinct subunits of 54 000 and 59 000 molecular weight were resolved on SDS-polyacrylamide gels. The germinal vesicle was shown to contain little of the colchicine-binding activity of the mature egg. Minimum and maximum estimates of the percentage of microtubule protein to total mature egg protein gave values of 0.8 % and 5 %, respectively. It was concluded that a considerable pool of this protein exists in the eggs of Urechis caupo.
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