Isolation and characterization of two acyl-CoA-binding proteins from proembryogenic masses of Digitalis lanata Ehrh.
Two acyl-CoA-binding-protein (ACBP) isoforms were isolated from proembryogenic masses of Digitalis lanata Ehrh. by column chromatography and preparative HPLC. The ACBPs had molecular masses of 9926 and 9997 Da, respectively. Partial sequence data indicated high similarity to each other and to ACBPs of other plant species such as Ricinus communis, Brassica napus and Arabidopsis thaliana. The isolated ACBPs bound palmitoyl-CoA with high affinity as determined by isoelectric-point shift.
Metzner
M
M
Institut für Pharmazeutische Biologie, Martin-Luther-Universität Halle-Wittenberg, Halle/Saale, Germany. metzner@pharmazie.uni-halle.de
Ruecknagel
K P
KP
Knudsen
J
J
Kuellertz
G
G
Mueller-Uri
F
F
Diettrich
B
B
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D026261:Diazepam Binding Inhibitor; D004070:Digitalis / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010946:Plants, Medicinal; D010947:Plants, Toxic; D011485:Protein Binding; D016415:Sequence Alignment
D000214:Acyl Coenzyme A; D002352:Carrier Proteins; D026261:Diazepam Binding Inhibitor; D010940:Plant Proteins