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J. Biol. Chem., Vol. 261, Issue 20, 9282-9288, Jul, 1986
J Gray, R Justice, GM Nagel and EJ Carroll Jr
A major protein component of the gel-like, embryonic hyaline layer of
Strongylocentrotus purpuratus has been purified and characterized. The
protein retains the ability to form an insoluble gel in the presence of
specific divalent cations, a property characteristic of the hyaline
material. Using a light scattering assay developed to measure the initial
rate of hyalin gelation, we have been able to show that calcium alone is
capable of initiating this reaction but that calcium and magnesium are
synergistic in their effect. In the absence of divalent cations, the major
hyalin protein has a molecular weight of 9.2 +/- 0.5 X 10(5) and a
sedimentation coefficient of 11.6 S; these and other data indicate that the
protein assumes a very elongated, rod-like structure in solution. Smaller
amounts of two additional proteins, 8.8 and 6.5 S, are present in the
hyalin fraction when the jelly coat and vitelline layer are subjected to a
more stringent acid treatment early in the isolation procedure.
Resolution and characterization of a major protein of the sea urchin hyaline layer
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