Reference : Bovine pepsinogen A: Isolation and parial characterization of isoforms with high activity
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63833
Bovine pepsinogen A: Isolation and parial characterization of isoforms with high activity
English
Idrissa-Sidikou, D. [> >]
Remy, B. [> >]
Gerardin-Otthiers, Nicole mailto [Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie >]
Joris, Bernard mailto [Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes - Centre d'ingénierie des protéines >]
Beckers, Jean-François mailto [Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction >]
2005
Journal of Animal and Veterinary Advances
Yes (verified by ORBi)
International
1680-5593
1993-601X
[en] Bovine ; Pepsinogen A ; Characterization
[en] The goal of this study was to purify bovine pepsinogen by a simple method allowing the preparation of large amount of pure protein. The purified protein and antisera are needed to develop diagnostic methods for further investigations in animals susceptible of gastric disorders or helminthosis. Pepsinogen isoforms were separated from extracts of bovine fundic mucosa by ammonium sulfate precipitations and chromatography on DEAE and hydroxyapatite. The isoforms showed a high activity in indirect proteolytic assay. Sequence analysis gave the following amino acid sequence SVVKIPLVKK for fraction 1, 2 and SVVKIPLVKKKSLRQNLIENGKLKE for fraction 3. The Mass spectrometry revealed isoforms with different masses from 39,864 to 40,181 Da. The estimated organic phosphate content ranged from 0.98 to 3.9 moles of phosphate per molecule. The protocol, with few steps, gave consequent quantities of pure and active protein available for further studies including the development of RIA and ELISA as diagnostic tools in gastrointestinal diseases.
Researchers ; Professionals
http://hdl.handle.net/2268/63833
http://medwelljournals.com/abstract/?doi=javaa.2005.894.901

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