BAUMERT, A and MAIER, W and GROGER, D and DEUTZMANN, R (1994) PURIFICATION AND PROPERTIES OF ACRIDONE SYNTHASE FROM CELL-SUSPENSION CULTURES OF RUTA-GRAVEOLENS L. ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, 49 (1-2). pp. 26-32. ISSN 0939-5075,
Full text not available from this repository.Abstract
Acridone synthase has been purified from cell suspension cultures of Ruta graveolens using a combination of gel filtration and ion exchange chromatography. The purified enzyme has an apparent molecular weight of 69 kDa on gel filtration and a subunit structure on SDS-PAGE of 40 kDa. The apparent K-m-values are 10.64 mu M and 32.8 mu M for N-methylanthraniloyl-CoA and malonyl-CoA, respectively. Tryptic digestion of the homogeneous acridone synthase was performed. Seven of the peptides were chosen for microsequencing. The homology of the amino acid sequences from this particular polypeptide and corresponding peptides from chalcone synthase 3 from garden pea amounted to 76%.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CHALCONE SYNTHASE; BIOSYNTHESIS; QUANTITIES; ALKALOIDS; SEQUENCE; ACETATE; RUTACEAE; RUTA GRAVEOLENS; ACRIDONE SYNTHASE; MICROSEQUENCING; ALKALOIDS |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53610 |
Actions (login required)
 |
View Item |
