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B6db references: ppcacst

type Journal Article
authors Van der Straeten, D.; Van Wiemeersch, L.; Goodman, H. M.; Van Montagu, M.
title Purification and partial characterization of 1-aminocyclopropane-1-carboxylate synthase from tomato pericarp
journal Eur J Biochem
ui Ppcacst
year (1989)
volume 182
number 3
pages 639-47
keywords Amino Acid Sequence
abstract 1-Aminocyclopropane-1-carboxylate synthase was purified 5000-fold from LiCl-induced tomato fruit slices by conventional and high-performance liquid chromatography. The final preparation was estimated to be between 25% and 50% pure. Two-dimensional gel electrophoresis indicates that 1-aminocyclopropane-1-carboxylate synthase activity is associated with a 45-kDa polypeptide, with a pI of 5.8 +/- 0.2. The enzyme is inactivated both by its substrate, S-adenosyl-L-methionine (AdoMet) and by one of its products, 1-aminocyclopropane-1-carboxylate. Due to the extremely low abundance of the protein it was necessary to scale up the extraction in order to obtain reasonable amounts for sequence analysis. Therefore, 200 kg tomatoes were extracted on semi-industrial scale and 1-aminocyclopropane-1-carboxylate synthase purified. This yielded approximately 150 micrograms enzyme.
last changed 2008/04/25 17:36

B6db references