Refolding of fully reduced bovine pancreatic trypsin.
Refolding of bovine pancreatic trypsin was carried out. When starting with denatured S-S intact trypsin, the recovered activity attained was 95-100%. In contrast, the recovered activity after refolding denatured S-S reduced trypsin was considerably low compared with other proteases that have been worked with previously. Such low recovered activity was attributed to the small amount of fully reduced trypsin used as starting material for complete refolding. Taking this into account, a recovered activity of 86% could be achieved when using inhibitor-immobilized gels.
Ohshima
Yuji
Y
Department of Biomolecular Science, Faculty of Engineering, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
Suzuki
Yusuke
Y
Nakatani
Akihiro
A
Nohara
Daisuke
D
D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004983:Ethanolamines / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry / Q000379:methods; D010179:Pancreas / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013438:Sulfhydryl Compounds; D014357:Trypsin / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry; D014362:Trypsinogen / Q000737:chemistry
D004983:Ethanolamines; D013438:Sulfhydryl Compounds; D014361:Trypsin Inhibitors; D014362:Trypsinogen; C020283:diethanolamine; D014357:Trypsin