Abstract
Purified human liver α- l-fucosidase (EC 3.2.1.51) has been radioiodinated by a chloramine-T procedure to a specific activity of 3.7·10 6 dpm/μg protein without altering its apparent Michaelis constant for the 4-methylumbelliferyl substrate. This 125I-labelled α- l-fucosidase has been used in development of a competitive binding radioimmunoassay for α- l-fucosidase which can detect 1–2 ng of enzyme protein and has been employed to quantify the amount of α- l-fucosidase protein in the liver and spleen from a patient with fucosidosis. Less than 1% of the normal amount of α- l-fucosidase protein is present suggesting that normal amounts of catalytically inactive α- l-fucosidase are not found in this disease.
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.
