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KMID : 0378019890320020025
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New Medical Journal
1989 Volume.32 No. 2 p.25 ~ p.36
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Immunological Study of Isozyme Pattern of γ-Glutamyltransferase from Various Tissues
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Abstract
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This study is an interim report to investigate the method by which y-glutamyitransferase. (y-GT) in rat hepatoma can be distinguished from y-GT of various other tissues.
Isozymes (sialo and asialo form) were purified from renal, and hepatic tissues of noiaial adult rat to observe the isozyme pattern on polyacrylamide gel electrophoresis, and the cross reactivity between 6 isozymes including y-GT from neonatal rat kidney and rat hepatoma induced by 2-acetamidofluorene against anti-y-GT antiserum.
The following results were obtained.
1. y-GT was purified from adult rat kidney 620 fold with an yield of 20%, and the final specific activity was 682 units per mg of protein. y-GT was purified from adult rat liver 782 fold with an yield of 4-7%, and the final specific activity was 5.1 units per mg of protein.
2. On Con A-Sepharose chromatography, sialo y-GTs from adult rat kidney and liver accounted for 6 3%, and 5.1% of the total y-GT respectively.
3. On 5-20% gradient polyacrylamide gel electrophoresis, sialo y-GT from adult rat kidney was observed to contain one fraction, and asialo form, two fractions, and both of asialo and sialo y-GTs from adult rat liver, one fraction.
It seemed that sialo and asialo y-GTs from adult rat kidney and liver differ from each other with respect to electrophoretic mobility and Con A-binding capacity.
4. In double immunodiffusion analysis, asialo y-GT from adult rat kindey showed similar immunogenicity to asialo y-GT from adult rat liver, and Asialo y-GTs from hepatoma and neonatal kidney, and sialo y-GTs from adult rat liver and kidney have cross reactivity against anti-y-GT antiserum.
Antibody-y-GT complex retains catalytic activity.
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KEYWORD
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