Abstract
Lectin from the bulbs of Cyclamen mirabile which is an endemic species of Turkey was successfully isolated by affinity precipitation with alginate in one step. The purified protein produced two bands showing a dimeric structure in SDS-PAGE (13.5 and 14.8 kDa). C. mirabile lectin showed activity and stability in a broad pH scale and kept its haemagglutination activity in the temperature range of 4-40°C. MgCl2 and HgCl2 inhibited the haemagglutination activity of the lectin. In this study, a practical and efficient purification procedure was carried out for C. mirabile lectin by using affinity precipitation with alginate.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Bilecik Şeyh Edebali Üniversitesi Fen Bilimleri Dergisi
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
