HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion
HCE, a constituent protease of the hatching enzymes of Oryzias latipes embryos [1,2], releases unique proline-rich polypeptides from its natural substrate, the hardened chorion. The polypeptides consist of repeats of Pro-X-Y, mainly Pro-Glx-X. In addition, the polypeptides contain abundant γ-glutamy...
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Veröffentlicht in: | FEBS letters 1994-02, Vol.339 (3), p.281-284 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | HCE, a constituent protease of the hatching enzymes of
Oryzias latipes embryos [1,2], releases unique proline-rich polypeptides from its natural substrate, the hardened chorion. The polypeptides consist of repeats of Pro-X-Y, mainly Pro-Glx-X. In addition, the polypeptides contain abundant γ-glutamyi ϵ-lysine isopeptides which are regarded to be responsible for chorion hardening. These findings suggest that HCE recognizes specific site(s) of the chorion, releases the proline-rich polypeptides from it, and makes the substrate accessible to LCE, another protease of the hatching enzymes. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(94)80431-1 |