Abstract
The protein composition of the sea urchin embryo hyaline layer has been studied by 125I surface labeling. The electrophoretic patterns of iodinated proteins indicate that the composition of the hyaline layer is species and stage-specific. Dissociation of iodinated embryos removes some labeled proteins of apparent molecular weights of 290,000, 175,000, 145,000, 110,000, 70,000, and 50,000. The electrophoretic pattern of labeled proteins found in the intact embryo is reestablished on the surface of aggregates following reaggregation. The possible function of these proteins with respect to cell adhesion, cell-sorting behavior and morphogenesis is discussed.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
