Article (Scientific journals)
Isolation of pregnancy-associated glycoproteins of the American bison (Bison bison) at first half of pregnancy
Kiewisz, J.; Melo de Sousa, Noelita; Beckers, Jean-François et al.
2008In General and Comparative Endocrinology, 155 (1), p. 164-175
Peer Reviewed verified by ORBi
 

Files


Full Text
KiewszJ_GeneralComparativeEndocrinology_2008.pdf
Publisher postprint (927.11 kB)
Demander un tiré à part
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
American bison; AmbPAGs; cotyledons; PAG; placenta
Abstract :
[en] This paper describes the successful purification and characterisation of pregnancy-associated glycoproteins (PAG) extracted from placenta (3-4 months) of American bisons (Amb). Chorionic AmbPAG proteins were purified from foetal cotyledonary tissues (CT) and liquid cotyledonary-carrying proteins (LCP) leaking from damaged cells. Our protocols successfully indicated the usefulness of AmbPAG protein identification, especially from LCP fraction. The AmbPAGs were extracted, precipitated and eluted during DEAE cellulose chromatography. The richest protein fractions were further chromatographed on VVA (Vicia villosa agglutinin affinity column), then characterised by mono- and bi-dimensional electrophoresis, Western blot and N-terminal amino acid (aa) sequence. After being transferred to PVDF membranes, three selected VVA-purified AmbPAG isoforms differing in molecular masses and isoelectric points (Ip 4-4.6) were selected for sequencing. One identified N-terminal 25 aa sequence of AmbPAG72 kDa CT form was identified as completely new (RGSNI_TSLPLQNVIDLFYVGNITIG). Two other AmbPAG proteins purified from different sources (74 kDa CT and 76 kDa LCP forms; RGSNLTIHPLRNIRDIFYVGNITIG) were identical or corresponded to N-terminus of various bovine PAGs (boPAG). The two AmbPAGs (74 kDa CT and 76 kDa LCP) revealed identical micro-sequence to boPAG7; and were similar mainly to bovine PAG4, -6, -15 and -17 precursors that were identified by full-length sequencing derived from cDNA cloning. The novel sequence of the AmbPAG (72 kDa CT) was related to some boPAG and various other ruminant PAG precursors (caprine and ovine). All three identified AmbPAG sequences were also relatively similar to mature forms of purified native boPAG56-75kDa proteins. This is the first report indicating aa sequences of native AmbPAG proteins purified from placenta (CT and LCP) of bison species. The N-terminal sequences of the AmbPAGs have been deposited in the EMBL-EBI database (UniProtKB; Accession Nos.: P84916, P84917 and P84918). (C) 2007 Elsevier Inc. All rights reserved.
Disciplines :
Veterinary medicine & animal health
Author, co-author :
Kiewisz, J.
Melo de Sousa, Noelita ;  Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction
Beckers, Jean-François  ;  Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction
Vervaecke, H.
Panasiewicz, G.
Szafranska, B.
Language :
English
Title :
Isolation of pregnancy-associated glycoproteins of the American bison (Bison bison) at first half of pregnancy
Publication date :
01 January 2008
Journal title :
General and Comparative Endocrinology
ISSN :
0016-6480
eISSN :
1095-6840
Publisher :
Elsevier, San Diego, United States - California
Volume :
155
Issue :
1
Pages :
164-175
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 08 March 2009

Statistics


Number of views
79 (5 by ULiège)
Number of downloads
0 (0 by ULiège)

Scopus citations®
 
29
Scopus citations®
without self-citations
10
OpenCitations
 
24

Bibliography


Similar publications



Contact ORBi