التفاصيل البيبلوغرافية
| العنوان: |
Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens |
| المؤلفون: |
Fujimura, Setsuo, Ueda, Ohmi, Shibata, Yukinaga, Hirai, Kaname |
| المصدر: |
FEMS Microbiology Letters; Feb2003, Vol. 219 Issue 2, p305, 5p |
| مصطلحات موضوعية: |
PEPTIDASE, ENZYME inhibitors |
| مستخلص: |
Prolyltripeptidyl amino peptidase activity was found in a crude extract of Prevotella nigrescens and this enzyme was purified by procedures including concentration with ammonium sulfate, ion exchange chromatography, gel filtration, and isoelectric focusing. This peptidase hydrolyzed Ala-Ala-Pro-p-nitroanilide as well as Ala-Phe-Pro-p-nitroanilide. Furthermore, several p-nitroanilide derivatives of dipeptides with a proline residue in the second position from the amino-terminal end (Xaa-Pro) were also cleaved detectably. The molecular mass of this tripeptidase was calculated as 56 kDa and its isoelectric point was 5.8. The enzyme was inactivated completely by heating at 60°C for 5 min and inhibited significantly by specific serine enzyme inhibitors. [Copyright &y& Elsevier] |
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| قاعدة البيانات: |
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