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Disulfide linkage patterns of pig zona pellucida glycoproteins ZP3 and ZP4
Author(s) -
Kanai S.,
Kitayama T.,
Yonezawa N.,
Sawano Y.,
Tanokura M.,
Nakano M.
Publication year - 2008
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.20836
Subject(s) - zona pellucida , glycoprotein , zona pellucida glycoprotein , biology , oocyte , cysteine , disulfide linkage , disulfide bond , biochemistry , microbiology and biotechnology , embryo , enzyme
Zona pellucida, a transparent envelope surrounding the mammalian oocyte, plays major roles in fertilization and consists of three or four glycoproteins. Primary structures, and especially the positions of cysteine (Cys) residues in the zona glycoproteins, are well conserved among mammals. In this study, we analyzed the disulfide linkages of pig ZP3 and ZP4 purified from ovaries. While disulfide linkage patterns of four Cys residues in the N‐terminal halves of the ZP domains of ZP3 and ZP4 were identical to those previously reported for mice, rats, humans, and fish, the disulfide linkage patterns of six Cys residues in the C‐terminal half of the ZP domain in ZP4, as well as eight Cys residues in the C‐terminal region of the ZP domain and a following region unique to ZP3, were different from those previously reported. Thus, higher‐order structures of zona glycoproteins might not be conserved in the C‐terminal regions. Mol. Reprod. Dev. 75: 847–856, 2008. © 2007 Wiley‐Liss, Inc.