Abstract
Abstract The mean rotational relaxation times of human macroglobulin (γM) conjugated with 1-dimethylaminonaphthalene-5-sulfonyl-chloride, its subunit (γMs), and its tryptic fragment (Fabµ) have been determined by the technique of polarization of fluorescence. Strikingly low values were found for γM (80 nsec) and γMs (69 nsec). These low values as well as other properties of γM and γMs are consistent with internal degrees of rotational freedom. The Fabµ fragment had a relaxation time indicative of a compact structure, and it is suggested that it may represent the effective rotational subunit in γM. Parallel studies with human 7 S γ2-globulin (γG) immunoglobulin and with its papain fragments yielded results and conclusions similar to those determined for γM and to those reported for γG of other species.
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.
