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

Zach Adam; Shimon Mayak

doi:10.1016/0014-5793(84)80870-4

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

Institute of Plant Sciences and Genetics in Agriculture

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	47-50
Number of pages	4
Journal	FEBS Letters
Volume	172
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(84)80870-4
State	Published - 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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10.1016/0014-5793(84)80870-4

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

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.",

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AU - Mayak, Shimon

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AB - 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.

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

Abstract

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Keywords

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