Purification and Determination of Inhibitory Activity of Recombinant Soyacystatin Against Papain and Fish Protease
Abstract
Recombinant (r-) soyacystatin was characterized for its inhibitory activity against papain and compared to egg white cystatin. r-Soyacystatin expressed in E. coli was purified with phenyl-Sepharose and DEAE 4.33 fold as a recombinant protein. Egg white cystatin was purified by using affinity chromatography on cm-papain-Sepharose. Inhibitory activity of r-soyacystatin was similar to that of egg white cystatin. The amount required to inhibit 50% activity of papain used in the assay, 2 pg, was 0.245 |ig and 0.310 jag for soyacystatin and egg white cystatin, respectively. r-Soyacystatin inhibited 90% of autolytic activity in fish muscle.
Rekombinant Soyasistatinin Saflaştırılması ve Papaine ve Balık Proteazlanna Karşı inhibitor Aktivitesinin Saptanması
Abstract
Rekombinant (r-) soyasistatinin papaine olan inhibitor aktivitesi karakterize edilerek yumurta beyazı sistatini ile karşılaştırılmıştır. E.coli de sentezlenen r-soyasistatin 4.33 kez saf rekombinant protein biçiminde phenyl-Sepharose ve DEAE kolonları ile saflaştırılın ıştır. Yumurta beyazı sistatin ise cm-papain-sepharose afınite kromatograflsi kullanılarak saflaştırılmıştır. Araştırmada, 2 (ig papainiıı %50 sini inhibe etmek için gereken soyasistatin miktarı 0.245 pg ve yumurta beyazı sistatin miktarı ise 0.310 pg dır. r-Soyasıstatın araştırmada kullanılan balık kasındaki otolitik aktivitenin %90 nu inhibe etmiştir.
Details
| Primary Language | Turkish |
|---|---|
| Journal Section | Research Articles |
| Authors | |
| Publication Date | June 1, 2004 |
| Published in Issue | Year 2004 Volume: 2004 Issue: 1 |
