ArticleFish physiology and biochemistry2011
Purification and characterization of pepsinogens and pepsins from the stomach of rice field eel (Monopterus albus Zuiew).
Article in Fish physiology and biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 20 citations in OpenAlex.
- Assessing seasonal changes in the efficiency of protein digestion in gastric and agastric fish using in vitro models.Fish physiology and biochemistry · 2026Article
- Evaluation of the Antiviral Activity of a Natural Product, Schisandrin B, Against Rhabdovirus Infection in Chinese Rice Field Eels.International journal of molecular sciences · 2026Article
- Accessing the reproducibility and specificity of pepsin and other aspartic proteases.Biochimica et biophysica acta · 2013Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Three pepsinogens (PG1, PG2, and PG3) were highly purified from the stomach of freshwater fish rice field eel (Monopterus albus Zuiew) by ammonium sulfate fractionation and chromatographies on DEAE-Sephacel, Sephacryl S-200 HR. The molecular masses of the three purified PGs were all estimated as 36 kDa using SDS-PAGE. Two-dimensional gel electrophoresis (2D-PAGE) showed that pI values of the three PGs were 5.1, 4.8, and 4.6, respectively. All the PGs converted into corresponding pepsins quickly at pH 2.0, and their activities could be specifically inhibited by aspartic proteinase inhibitor pepstatin A. Optimum pH and temperature of the enzymes for hydrolyzing hemoglobin were 3.0-3.5 and 40-45 °C. The K (m) values of them were 1.2 × 10⁻⁴ M, 8.7 × 10⁻⁵ M, and 6.9 × 10⁻⁵ M, respectively. The turnover numbers (k(cat)) of them were 23.2, 24.0, and 42.6 s⁻¹. Purified pepsins were effective in the degradation of fish muscular proteins, suggesting their digestive functions physiologically.
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