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. 1992 Jun;99(2):751–754. doi: 10.1104/pp.99.2.751

Extraction and Partial Characterization of the Ethylene-Forming Enzyme from Apple Fruit 1

J Carlos Fernández-Maculet 1, Shang Fa Yang 1
PMCID: PMC1080528  PMID: 16668949

Abstract

Ethylene-forming enzyme (EFE) was isolated from apple (Malus domestica Borkh. cv Golden Delicious) fruit tissue. The enzyme activity in the homogenate is associated with the pellet fraction and can be solubilized with Triton X-100 or polyvinylpolypyrrolidone. The solubilized enzyme system resembles the in vivo system in that it exhibits a low Km (17 micromolar) for its substrate 1-aminocyclopropane-1-carboxylic acid (ACC), is stereospecific toward 2-ethyl-ACC stereoisomers for 1-butene production, and is inhibited by cobalt ions and α-aminoisobutyric acid. Intact preclimacteric fruits treated with exogenous ethylene showed a marked increase in in vivo EFE activity and this increase was accompanied by a parallel increase in in vitro EFE activity. These results support the notion that the isolated EFE represents the authentic in vivo activity.

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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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