Lectin Affinity Electrophoresis

Author(s):  
Yuka Kobayashi
1993 ◽  
Vol 39 (7) ◽  
pp. 1404-1407 ◽  
Author(s):  
M Mattiazzo ◽  
I Ramasamy

Abstract We have modified a commercially available procedure involving precast agarose gels (Paragon Isopal System) to measure alkaline phosphatase (EC 3.1.3.1) isoenzymes. Including wheat germ lectin in the equilibration buffer improved the resolution of the bone and liver isoenzymes. Unlike previously described wheat germ lectin affinity electrophoresis methods, the procedure measures bone, liver, and biliary isoenzymes in a single step. There was good correlation between the affinity electrophoresis and the neuraminidase preincubation methods for the measurement of bone (r = 0.958) and liver (r = 0.962) alkaline phosphatase isoenzymes. However, the affinity electrophoresis method also quantified minor isoenzyme fractions that were poorly resolved by the neuraminidase method. The method is technically simple, reproducible, and capable of rapid handling of large workloads.


1986 ◽  
Vol 884 (1) ◽  
pp. 158-165 ◽  
Author(s):  
Catherine A. Hanham ◽  
A.John Chapman ◽  
Michael C. Sheppard ◽  
Elizabeth G. Black ◽  
D.B. Ramsden

1993 ◽  
Vol 214 (1) ◽  
pp. 3-12 ◽  
Author(s):  
Kayoko Shimizu ◽  
Tomoko Taniichi ◽  
Shinji Satomura ◽  
Shuji Matsuura ◽  
Hiroko Taga ◽  
...  

1992 ◽  
Vol 604 (1) ◽  
pp. 91-94 ◽  
Author(s):  
Hidematsu Hirai ◽  
Kazuhisa Taketa

1989 ◽  
Vol 10 (12) ◽  
pp. 825-829 ◽  
Author(s):  
Kazuhisa Taketa ◽  
Eriko Ichikawa ◽  
Jiro Sato ◽  
Hiroko Taga ◽  
Hidematsu Hirai

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