Journals / Gaziosmanpaşa Üniversitesi Ziraat Fakültesi Dergisi / 2004 / Cilt: 2004 Sayı: 1

Purification and Determination of Inhibitory Activity of Recombinant Soyacystatin Against Papain and Fish Protease

Rekombinant Soyasistatinin Saflaştırılması ve Papaine ve Balık Proteazlanna Karşı inhibitor Aktivitesinin Saptanması

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Publication Date
2004-06-01
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⚡ TL;DR(Too Long; Didn't Read)

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.

📌 3 Key Takeaways

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Objective & Hypothesis: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.
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Key Findings & Data:Egg white cystatin was purified by using affinity chromatography on cm-papain-Sepharose.
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Conclusion & Impact: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.
🔬Design:Makale
📍Scope:Comprehensive Sample
⚙️Variables:Soyasistatin yumurta beyazı sistatin proteolitic aktivite protein saflaştırma · soyacystatin egg white cystatin proteolytic activity protein purification

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.

Özet

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.

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Cite This Article

Akpınar, Ö. (2004). Purification and Determination of Inhibitory Activity of Recombinant Soyacystatin Against Papain and Fish Protease. Gaziosmanpaşa Üniversitesi Ziraat Fakültesi Dergisi, Cilt: 2004 Sayı: 1. https://ajindex.com/articles/1208585

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