Reference : Isolation of pregnancy-associated glycoproteins of the American bison (Bison bison) a...
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
http://hdl.handle.net/2268/7992
Isolation of pregnancy-associated glycoproteins of the American bison (Bison bison) at first half of pregnancy
English
Kiewisz, J. [> > > >]
Melo de Sousa, Noelita mailto [Université de Liège - ULg > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Beckers, Jean-François mailto [Université de Liège - ULg > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Vervaecke, H. [> > > >]
Panasiewicz, G. [> > > >]
Szafranska, B. [> > > >]
1-Jan-2008
General and Comparative Endocrinology
Elsevier
155
1
164-175
Yes (verified by ORBi)
International
0016-6480
San Diego
[en] American bison ; AmbPAGs ; cotyledons ; PAG ; placenta
[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.
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http://hdl.handle.net/2268/7992

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