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Isolation and partial characterization of three pregnancy‐associated glycoproteins from the ewe placenta
Author(s) -
El Amiri Bouchra,
Remy Benoit,
Sousa Noelita Melo,
Joris Bernard,
Ottiers Nicole Gerardin,
Perenyi Zsolt,
Mboko Henri Banga,
Beckers JeanFrancois
Publication year - 2003
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.10246
Subject(s) - biology , glycoprotein , placenta , peptide sequence , gene isoform , biochemistry , molecular cloning , microbiology and biotechnology , antiserum , molecular mass , amino acid , cloning (programming) , fetus , pregnancy , gene , genetics , enzyme , antibody , computer science , programming language
Pregnancy‐associated glycoproteins (PAGs) are synthesized in the outer epithelial layer of the placenta in artiodactyls. In this work, three novel ovine PAGs were isolated from late‐pregnancy fetal cotyledons and characterized biochemically. The isolation procedure included acid and ammonium sulfate precipitations and anion and cation exchange chromatographies. The isolated PAGs have different NH 2 ‐terminal amino acid sequences (RGSXLTILPLRNMRDIVY, ISRVSXLTIHPLRNIMDML, and RGSNLTIHPLRNIRD) and apparent molecular masses (55, 57, and 59 kDa). Each shows several isoforms with different pI values. The three proteins share high sequence identity with each other and with other ovine, bovine, and caprine PAGs. They have not been described previously. The ovPAG‐59 sequence differs from the previously identified ovPAG‐4 sequence (determined by DNA cloning and sequencing) at only one position among the 15 N‐terminal residues. The newly characterized ovPAGs and the procedure used to isolate them will be helpful in producing new antisera for investigating PAG secretion in pregnant ewes. Mol. Reprod. Dev. 64: 199–206, 2003. © 2003 Wiley‐Liss, Inc.