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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
Author(s) -
Lee Kyong-Su,
Yasumasu Shigeki,
Nomura Kohji,
Iuchi Ichiro
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80431-1
Subject(s) - oryzias , hatching , protease , enzyme , proline , substrate (aquarium) , biochemistry , embryo , biology , substrate specificity , chemistry , amino acid , microbiology and biotechnology , ecology , gene
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.