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+ subs
Apical localization of 1-aminocyclopropane-1-carboxylic acid and its conversion to ethylene in etiolated pea seedlings
β Scribed by J. E. Taylor; D. G. Grosskopf; B. A. McGaw; R. Horgan; I. M. Scott
- Publisher
- Springer-Verlag
- Year
- 1988
- Tongue
- English
- Weight
- 295 KB
- Volume
- 174
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
The biosynthetic basis for the high rates of ethylene production by the apical region of etiolated pea (Pisum sativum L.) seedlings was investigated. The ethylene precursor l-aminocyclopropane-l-carboxylic acid (ACC) was quantified in extracts of various regions of seedlings by measuring isotopic dilution of a 2H-labelled internal standard using selected-ion-monitoring gas chromatography/mass spectrometry. The ACC levels in the apical hook and leaves were much higher than in the expanded internodes of the epicotyl. The capacity of excised tissue sections to convert exogenous ACC to ethylene was also much greater in the apical region, reflecting the distribution of soluble protein in the epicotyl.
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