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The Journal of Cell Biology, Vol 44, 611-617, Copyright © 1970 by Rockefeller University Press

ARTICLE

SOME PROPERTIES OF HYALIN : The Calcium-Insoluble Protein of the Hyaline Layer of the Sea Urchin Egg



R. E. Stephens 1 and R. E. Kane 1

1 From the Department of Biology, Brandeis University, Waltham, Massachusetts 02154; the Pacific Biomedical Research Center, University of Hawaii, Honolulu, Hawaii 96822; and The Marine Biological Laboratory, Woods Hole, Massachusetts 02543

The principal protein component of the hyaline layer of sea urchin eggs is the calcium-insoluble protein first described by Kane and Hersh. The protein hyalin is abnormally high in acidic amino acids, almost devoid of basic amino acids, and characteristically rich in valine and proline. Essentially all of the cysteine present is found in the disulfide form; no evidence points to intermolecular disulfide linkages. Hyalin from several species has a minimal subunit weight of about 100,000, though evidence exists for a particle three times this weight in urea or guanidine hydrochloride from one species. Optical rotatory dispersion measurements indicate no alpha-helix content, though the dispersion has unique characteristic features. Addition of small quantities of calcium causes hyalin to gel to a birefringent fibrous form. The fibrous, birefringent form of hyalin is rendered isotropic upon addition of EDTA, but the birefringence is restored with re-addition of divalent cation.

Submitted on August 27, 1969
Revised on October 25, 1969


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