http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
The Partial Purification and Properties of Pepsin Obtained from Turkey Proventriculus
Temiz, Hasan,Aykut, Umut,Okumus, Emin,Turhan, Sadettin Korean Society for Biotechnology and Bioengineerin 2007 Biotechnology and Bioprocess Engineering Vol.12 No.4
In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SOS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results.
The Partial Purification and Properties ofPepsin Obtained from Turkey Proventriculus
Sadettin Turhan,Hasan Temiz,Umut Aykut,Emin Okumus 한국생물공학회 2007 Biotechnology and Bioprocess Engineering Vol.12 No.4
In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SDS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results.