Differentiation of scombroid fish species (tunas, bonitos and mackerels) by isoelectric focusing, titration curve analysis and native polyacrylamide gel electrophoresis of sarcoplasmic proteins

1995 ◽  
Vol 16 (1) ◽  
pp. 820-822 ◽  
Author(s):  
Hartmut Rehbein
Keyword(s):  
Isoelectric Focusing ◽  
Fish Species ◽  
Titration Curve ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Curve Analysis ◽  
Polyacrylamide Gel ◽  
Sarcoplasmic Proteins ◽  
Native Polyacrylamide Gel Electrophoresis

scholarly journals Antibody-affinity purification of novel α-l-fucosidase from mouse liver

1987 ◽  
Vol 245 (2) ◽  
pp. 589-593 ◽  
Author(s):  
L D Laury-Kleintop ◽  
I Damjanov ◽  
J A Alhadeff
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Human Liver ◽  
Mouse Liver ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Antibody Affinity ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Sepharose 4B

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.

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