Purification and partial characterization of canine pepsinogen A and B

Jan S. Suchodolski, Jörg M. Steiner, Craig G. Ruaux, Andrea Boari, David A. Williams

Research output: Contribution to journalArticlepeer-review


Objective - To purify and partially characterize various isoforms of canine pepsinogen (PG) from gastric mucosa. Sample Population - Stomachs obtained from 6 euthanatized dogs. Procedure - Mucosa was scraped from canine stomachs, and a crude mucosal extract was prepared and further purified by use of weak anion-exchange chromatography, hydroxyapatite chromatography, size-exclusion chromatography, and strong anion-exchange chromatography. Pepsinogens were characterized by estimation of molecular weights, estimation of their isoelectric points (IEPs), and N-terminal amino acid sequencing. Results - Two different groups of canine PG were identified after the final strong anion-exchange chromatography: PG A and PG B. Pepsinogens differed in their molecular weights and IEP Pepsinogen B appeared to be a dinner with a molecular weight of approximately 34,100 and an IEP of 4.9. Pepsinogen A separated into several isoforms. Molecular weights for the various isoforms of PG A ranged from 34,200 to 42,100, and their IEPs ranged from 4.0 to < 3.0.The N-terminal amino acid sequence for the first 25 amino acid residues for PG A and B had good homology with the amino acid sequences for these proteins in other species. Conclusions and Clinical Relevance - Canine PG B and several isoforms of canine PG A have been purified. Availability of these PGs will facilitate development of immunoassays to measure PG in canine serum as a potential diagnostic marker for gastric disorders in dogs.

Original languageEnglish (US)
Pages (from-to)1585-1590
Number of pages6
JournalAmerican journal of veterinary research
Issue number11
StatePublished - Nov 1 2002
Externally publishedYes

ASJC Scopus subject areas

  • veterinary(all)


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