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HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion.

作者信息

Lee K S, Yasumasu S, Nomura K, Iuchi I

机构信息

Life Science Institute, Sophia University, Tokyo, Japan.

出版信息

FEBS Lett. 1994 Feb 21;339(3):281-4. doi: 10.1016/0014-5793(94)80431-1.

Abstract

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 gamma-glutamyl epsilon-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.

摘要

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