Abstract
Abstract: α.-Fetoprotein samples isolated from human cord serum by metal affinity chromatography and immunoaffi.nity method were compared by circular dichroism, fluorescence spectroscopy and scanning microcalorimetry. The isolation procedures were quite distinguished by their influence on native protein structure (and, consequently, by the effectiveness of natural ligand release from a protein molecule). As a result, structural properties and conformational stability of a.-fetoprotein in the samples were found to be rather different.
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.
