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. 1980 May 1;187(2):329–335. doi: 10.1042/bj1870329

Reactivation in vitro of zinc-requiring apo-enzymes by rat liver zinc-thionein

Albert O Udom 1, Frank O Brady 1
PMCID: PMC1161797  PMID: 6772158

Abstract

The ability of rat liver zinc-thionein to donate its metal to the apo-enzymes of the zinc enzymes horse liver alcohol dehydrogenase, yeast aldolase, thermolysin, Escherichia coli alkaline phosphatase and bovine erythrocyte carbonic anhydrase was investigated. Zinc-thionein was as good as, or better than, ZnSO4, Zn(CH3CO2)2 or Zn(NO3)2 in donating its zinc to these apo-enzymes. Apo-(alcohol dehydrogenase) could not be reactivated by zinc salts or by zinc-thionein. Incubation of the other apo-enzymes with near-saturating amounts of zinc as ZnSO4, Zn(CH3CO2)2, Zn(NO3)2, or zinc-thionein resulted in reactivation of the apo-enzymes. With apo-aldolase zinc-thionein gave 100% reactivation within 30min. Reactivation by ZnSO4 and Zn(CH3CO2)2 was complete and instantaneous. Zinc-thionein was somewhat better than Zn(NO3)2 in completely reactivating apo-thermolysin. With apo-(alkaline phosphatase) 43% reactivation was obtained with Zn(CH3CO2)2 and 18% with zinc-thionein. With apo-(carbonic anhydrase) zinc-thionein was better than ZnSO4, Zn(CH3CO2)2 or Zn(NO3)2, with a maximal reactivation of 54%. That zinc was really being transferred from zinc-thionein to apo-(carbonic anhydrase) was shown by the fact that 2,6-pyridine dicarboxylic acid and 1,10-phenanthroline had minimal effects on the reactivation of apo-(carbonic anhydrase) when added after the incubation {[apo-(carbonic anhydrase)+zinc thionein]+chelator}, but inhibited reactivation when added before the incubation {apo-(carbonic anhydrase)+[zinc-thionein+chelator]}. These observations support the idea that zinc-thionein can function in zinc homeostasis as a reservoir of zinc, releasing the metal to zinc-requiring metalloenzymes according to need.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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