Abstract:
:Chalcone synthase was purified to homogeneity by polyacrylamide gel electrophoresis from cell suspension cultures of carrot in which anthocyanin synthesis was induced by transferring the cells from a medium containing 2,4-dichlorophenoxy-acetic acid (2,4-D) to one lacking it. A molecular weight of 80,000-85,000 for the enzyme was determined by gel filtration and disc-gel polyacrylamide electrophoresis, and one of about 40,600 for the subunit by SDS slab-gel electrophoresis. The primary reaction product was chalcone and the pH optimum of the reaction was 8.0. The Km values for 4-coumaroyl-CoA and malonyl-CoA were 5.7 microM and 18 microM, respectively. These properties of carrot chalcone synthase were discussed in comparison to those of that from cell cultures of parsley reported previously. Antiserum against chalcone synthase from carrot was obtained from mice bred under specific pathogen free conditions. Crossreactivity was examined by Western-blotting, and the high specificity of the antiserum against chalcone synthase was demonstrated.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Ozeki Y,Sakano K,Komamine A,Tanaka Y,Noguchi H,Sankawa U,Suzuki Tdoi
10.1093/oxfordjournals.jbchem.a135278subject
Has Abstractpub_date
1985-07-01 00:00:00pages
9-17issue
1eissn
0021-924Xissn
1756-2651journal_volume
98pub_type
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