Enzymatic ethylene formation from 1-aminocyclopropane-1-carboxylic acid by manganese, a protein fraction and a cofactor of etiolated pea shoots

✍ Scribed by Jörg R. Konze; Gertrud M. K. Kwiatkowski

• Publisher: Springer-Verlag
• Year: 1981
• Tongue: English
• Weight: 657 KB
• Volume: 151
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00393285

✦ Synopsis

The cofactor of enzymatic, 1-aminocyclopropane-l-carboxylic acid dependent ethylene formation was concentrated on cation exchange columns. When chelators of cations were added to the homogenares, cofactor activity was lost. Cofactor fractions were partly resistant to oxidation at 600 ~ C. Mn 2+ substituted for the cofactor in ethylene formation from 1-aminocyclopropane-l-carboxylic acid by a protein fraction isolated from etiolated pea shoots. In addition, Mn 2+ enhanced the stimulatory effect of the concentrated cofactor. The elution volume for the cofactor on a Sephadex G-25 column was lower than that of MnCI2. In paper electrophoresis the cofactor migrated to the cathode at pH 10.8 and 2.2. The Rv of cofactor on cellulose plates developed in butanol:acetic acid:H20 was 0.4. After cellulose chromatography, cofactor activity had to be reconstituted by the addition of MnC1 z. Chelators, anti-oxidants, and catalase were inhibitors of Mn 2 +-cofactordependent ethylene formation. The protein necessary for 1-aminocyclopropane-l-carboxylic acid dependent ethylene formation in vitro was seperated from 95 98% of the total protein in homogenates by DE-52 cellulose chromatography and (NH4)zSOg-fractionation.