Antibody-affinity purification of novel alpha-L-fucosidase from mouse liver.
Publication/Presentation Date
7-15-1987
Abstract
Previous studies have documented the presence of a novel alpha-L-fucosidase in mouse liver that contains unique basic isoelectric forms and that is antigenically similar to, but not identical with, human liver alpha-L-fucosidase [Laury-Kleintop, Damjanov & Alhadeff (1985) Biochem. J. 230, 75-82]. In the present investigation, mouse liver alpha-L-fucosidase was purified approx. 26,500-fold in 10% overall yield by antibody-affinity chromatography with the IgG fraction of goat anti-(human alpha-L-fucosidase) antibody coupled to Sepharose 4B. Native polyacrylamide-gel electrophoresis and SDS/polyacrylamide-gel electrophoresis indicated that the mouse fucosidase is highly purified if not homogeneous. Isoelectric focusing demonstrated that all enzymic forms found in crude mouse liver supernatant fluids were purified by the antibody-affinity procedure.
Volume
245
Issue
2
First Page
589
Last Page
593
ISSN
0264-6021
Published In/Presented At
Laury-Kleintop, L. D., Damjanov, I., & Alhadeff, J. A. (1987). Antibody-affinity purification of novel alpha-L-fucosidase from mouse liver. The Biochemical journal, 245(2), 589–593. https://doi.org/10.1042/bj2450589
Disciplines
Medicine and Health Sciences
PubMedID
3663178
Department(s)
Department of Medicine
Document Type
Article