Inhibitory effect of thyroxine on carbonic anhydrase B isozyme biosynthesis in rabbit reticulocyte lysates
1978; Elsevier BV; Volume: 85; Issue: 3 Linguagem: Inglês
10.1016/0006-291x(78)90636-8
ISSN1090-2104
AutoresNaoyuki Taniguchi, Naoki Ishikawa, Takahito Kondo,
Tópico(s)Amino Acid Enzymes and Metabolism
ResumoBiosynthesis of rabbit red cell carbonic anhydrase isozyme B and C was demonstrated in reticulocyte cell-free lysates by the specific immunoprecipitin reaction. Using this homologous protein synthesis system, it was found that 10−5 to 10−7 M thyroxine preferentially inhibited the synthesis of carbonic anhydrase B isozyme without affecting that of C isozyme. These results suggested that this inhibitory action of the protein synthesis by thyroxine may be responsible for the decreased level of the B type isozymes in human hyperthyroidism or experimental hyperthyroidism of rabbits.
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