A novel purification procedure for chalcone flavanone isomerase from Petunia hybrida and the use of its antibodies to characterize the Po mutation
- 1 August 1987
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 257 (1) , 85-91
- https://doi.org/10.1016/0003-9861(87)90545-5
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- THE PHYTOALEXIN RESPONSE: ELICITATION, SIGNALLING AND CONTROL OF HOST GENE EXPRESSIONBiological Reviews, 1986
- Molecular cloning of the c2 locus of Zea mays, the gene coding for chalcone synthaseMolecular Genetics and Genomics, 1986
- Structure of the chalcone synthase gene of Antirrhinum majusMolecular Genetics and Genomics, 1986
- Floral tissue ofPetunia hybrida(V30) expresses only one member of the chalcone synthase multigene familyNucleic Acids Research, 1986
- Cloning and analysis of two genes for chalcone synthase from Petunia hybridaMolecular Genetics and Genomics, 1985
- Chalcone isomerase in flowers of mutants of Petunia hybridaPlanta, 1983
- Highly purified “flavanone synthase” from parsley catalyzes the formation of naringenin chalconeArchives of Biochemistry and Biophysics, 1980
- Genetic control of chalcone isomerase activity in anthers of Petunia hybridaPlanta, 1979
- Comparison of chalcone-flavanone isomerase heteroenzymes and isoenzymesPhytochemistry, 1970
- Purification and properties of chalcone-flavanone isomerase from soya bean seedPhytochemistry, 1967