Abstract
The enzyme formate dehydrogenase (FDH) was purified from the crude extract of Candida boidinii by affinity partition chromatography. The partition coefficient, K, of the enzyme was selectively increased by adding polyethylene glycol—Procion Red HE3b as an affinity ligand to the mobile phase in the chromatographic column. The increased K value led to early elution of the enzyme—ligand complex and separated the target protein from the main peak of the contaminants.
Sign-in/Register to access full text options 
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 callDisclaimer: 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.
