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Antisera were raised in rabbits against native and sodium dodecylsulfate denatured forms of human acid alpha-glucosidase and beta-hexosaminidases A and B. Anti-native enzyme antisera were able to precipitate all or nearly all enzyme activity from cell extracts, and to eliminate all stainable activity on electrophoresis. Antisera prepared against denatured enzymes precipitated only a minor part of enzyme activity. Electrophoretic analysis showed that these antisera were able to bind to the enzyme molecule. The result was a slowing down of the anodic migration but not immobilization. The use of variants with hexosaminidase deficiencies helped to clarify the action of the antisera on the various hexosaminidase isozymes.
A M Besançon, and
S Gautron, and
L Poenaru, and
J C Dreyfus
June 1992,
American journal of veterinary research,
A M Besançon, and
S Gautron, and
L Poenaru, and
J C Dreyfus
August 2004,
Journal of dairy science,
A M Besançon, and
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J C Dreyfus
October 2000,
Die Nahrung,
A M Besançon, and
S Gautron, and
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J C Dreyfus
November 1998,
Journal of immunological methods,
A M Besançon, and
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September 1990,
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A M Besançon, and
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J C Dreyfus
May 1970,
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A M Besançon, and
S Gautron, and
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December 1976,
Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles,
A M Besançon, and
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March 1976,
Clinica chimica acta; international journal of clinical chemistry,
A M Besançon, and
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J C Dreyfus
June 2007,
Biochemical and biophysical research communications,
A M Besançon, and
S Gautron, and
L Poenaru, and
J C Dreyfus
November 1981,
Biochimica et biophysica acta,
