The partial purification and properties of pepsin obtained from Turkey proventriculus
| Autor: | Hasan Temiz, Sadettin Turhan, Emin Okumus, Umut Aykut |
|---|---|
| Přispěvatelé: | Ondokuz Mayıs Üniversitesi |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology Size-exclusion chromatography Biomedical Engineering Bioengineering Proventriculus enzyme purification gel filtration Turkey proventriculus Applied Microbiology and Biotechnology Electrophoresis Enzyme Column chromatography chemistry Pepsin Sephadex proteolytic activity biology.protein Centrifugation Biotechnology pepsin |
| DOI: | 10.1007/BF02931070 |
| Popis: | WOS: 000249227300019 In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SIDS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results. (c) KSBB. |
| Databáze: | OpenAIRE |
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