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Ribonucleoprotein-Bound Antibody to the Enzyme Triose Phosphate Dehydrogenase

From the Biology Division, Oak Ridge National Laboratory, ¹ Oak Ridge, Tennessee

Abstract

Microsomes prepared from the spleens and livers of mice immunized to the enzyme triose phosphate dehydrogenase have been found to possess inhibiting activity to enzymic function. Deoxycholate-treated microsomes had the same specific activity as intact microsomes, indicating that inhibiting activity was associated with the protein of ribonucleoprotein particles.

Serum-neutralizing antibody was adsorbed onto microsomes both in vitro and in vivo. Such adsorption could account for some of the inhibiting activity associated with microsomes. Treatment of the microsomes with deoxycholate, however, removed the artificially bound, neutralizing antibody.

Studies with -mercaptoethanol indicated that this sulfhydryl compound protected the enzyme from neutralizing activity of antisera or microsomal fractions but did not inhibit precipitate formation.

Footnotes

¹ Operated by Union Carbide Corporation for the United States Atomic Energy Commission.