Ontology highlight
ABSTRACT:
SUBMITTER: Van der Straeten D
PROVIDER: S-EPMC54218 | biostudies-other | 1990 Jun
REPOSITORIES: biostudies-other
Van der Straeten D D Van Wiemeersch L L Goodman H M HM Van Montagu M M
Proceedings of the National Academy of Sciences of the United States of America 19900601 12
1-Aminocyclopropane-1-carboxylate synthase (ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase, EC 4.4.1.14), the key enzyme in ethylene biosynthesis, was purified 5000-fold from induced tomato pericarp. ACC synthase activity was unambiguously correlated with a 45-kDa protein by two independent methods. Peptide sequences were obtained both from the N terminus after electroblotting and from tryptic peptides separated by reversed-phase chromatography. Mixed oligonucleotide probes were ...[more]