Solubilization and partial purification of an enzyme converting 1-aminocyclopropane-l-carboxylic acid to ethylene in plants

Zach Adam, Shimon Mayak*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The membrane-bound enzyme capable of catalyzing the conversion of 1-aminocyclopropane-1-carboxylic acid (ACC) to ethylene can be solubilized by treatment with detergent. The non-ionic detergent Nonidet P-40, at an optimum concentration of 0.2% and a protein : detergent ratio of 1:2, was found to be an effective solubilizer of the conversion activity. The solubilized enzyme resembles the membrane-bound enzyme with respect to heat sensitivity, pH dependence, Mn2+ stimulation and Co2+ inhibition. The enzyme can be further purified by means of ion-exchange chromatography with 12-fold increase in specific activity.

Original languageAmerican English
Pages (from-to)47-50
Number of pages4
JournalFEBS Letters
Volume172
Issue number1
DOIs
StatePublished - 25 Jun 1984

Bibliographical note

Funding Information:
This investigationw as supported by the US-Israel Binational Agricultural Research and DevelopmentF und (BARD) I-250-83.

Keywords

  • Ethylene 1-Aminocyclopropane-1-carboxylic acid Solubilization

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