Reference : Pregnancy-associated glycoprotein, chymosin and pepsinogen immunoreactivity of proteins ...
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
http://hdl.handle.net/2268/103772
Pregnancy-associated glycoprotein, chymosin and pepsinogen immunoreactivity of proteins extracted from fetal gastric tissue in bovine species.
English
Bella, Amina mailto [Université de Liège - ULg > > > Doct. sc. vété. (Bologne)]
Melo de Sousa, Noelita mailto [Université de Liège - ULg > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Dehimi, M. L. [> >]
Beckers, Jean-François mailto [Université de Liège - ULg > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Jun-2012
Research in Veterinary Science
British Veterinary Association
92
3
378-386
Yes (verified by ORBi)
International
0034-5288
London
United Kingdom
[en] Stomach ; foetus ; pregnancy-associated glycoprotein ; pepsinogen ; chymosin ; pepsinogen ; immunoreactivity
[en] The objective of this work was to investigate the expression of gastric aspartic proteinases in fundic and pyloric mucosa removed from bovine fetuses. For this purpose, fractions issued from classical biochemical protocols were analyzed by proteolytic method, by PAG-RIA and by Western blot with the use of antisera raised against both pepsinogens and PAG. A strong reaction of proteins extracted from the fundic mucosa collected at the beginning of pregnancy was revealed with both anti-bPAG-I and anti-bPAG-II antisera, suggesting the expression of pepsinogen F in bovine species. Concerning pyloric mucosa, the analysis by Western blot highlighted a very strong immunoreaction with the anti-bovine chymosin serum. Amino-terminal sequencing allowed to identify bovine fetuin and albumin in fundic extracts, chymosin in the pyloric mucosa extracts, as well as some unknown proteins in both mucosa. Despite no N-terminal microsequence corresponding to the hypothetical pepsinogen F could be identified, it cannot be excluded that an existing bovine pepsinogen F-like molecule could be degraded during the purification procedure or that co-purified proteins could be responsible for masking its N-terminal microsequence.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/103772
10.1016/j.rvsc.2011.03.023

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