Isoform, kinetic and immunochemical characterization of rodent liver alpha-L-fucosidases.
Publication/Presentation Date
1-1-1990
Abstract
alpha-L-Fucosidase from hamster and six inbred mouse strains contains two to three unique basic isoelectric forms (above pI 7.0) in addition to the usual acidic and neutral isoforms from pI 4-7. Rat liver alpha-L-fucosidase contains multiple isoforms between pI values of 4.0 and 7.3 whereas guinea pig liver alpha-L-fucosidase exhibits a single broad isoform at pI 5.3. 2. All the alpha-L-fucosidases have similar KM values (0.05-0.12 mM) for 4-methylumbelliferyl-alpha-L-fucopyranoside but pH-activity curves which are significantly different in optima and per cent of optimal activity in the acid region. 3. Double-antibody immunoprecipitation experiments indicate that rodent liver alpha-L-fucosidases crossreact to varying extents with polyclonal antibody against human liver alpha-L-fucosidase. 4. Hamster, guinea pig and mouse liver alpha-L-fucosidases exhibit significantly less binding than human and rat liver fucosidases to the agarose-epsilon-aminocaproylfucosamine affinity resin.
Volume
97
Issue
4
First Page
713
Last Page
717
ISSN
0305-0491
Published In/Presented At
Johnson, S. W., & Alhadeff, J. A. (1990). Isoform, kinetic and immunochemical characterization of rodent liver alpha-L-fucosidases. Comparative biochemistry and physiology. B, Comparative biochemistry, 97(4), 713–717. https://doi.org/10.1016/0305-0491(90)90112-7
Disciplines
Medicine and Health Sciences
PubMedID
2085955
Department(s)
Department of Medicine
Document Type
Article