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Rekombinant Soyasistatinin Saflaştırılması ve Papaine ve Balık Proteazlarına Karşı İnhibitor Aktivitesinin Saptanması

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

Journal Name:

  • Gaziosmanpaşa Üniversitesi Ziraat Fakültesi Dergisi

Publication Year:

  • 2004

Key Words:

Keywords (Original Language):

Author NameUniversity of AuthorFaculty of Author
Abstract (2. Language): 
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 ug, was 0.245 ug and 0.310 ug for soyacystatin and egg white cystatin, respectively. r-Soyacystatin inhibited 90% of autolytic activity m fish muscle.
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Abstract (Original Language): 
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 saflaştırılmıştır. Yumurta beyazı sistatin ise cm-papain-sepharose afınite kromatografisi kullanılarak saflaştırılmıştır. Araştırmada, 2 ug papainin %50 sini inhibe etmek için gereken soyasistatin miktarı 0.245 ug ve yumurta beyazı sistatin miktarı ise 0.310 ug dır. r-Soyasıstatın araştırmada kullanılan balık kasındaki otolitik aktivitenin %90 nu inhibe etmiştir.
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  • 1
19-26
  • Turkish

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