An affinity probe for isolation of abscisic acid-binding proteins.
An affinity probe has been developed for isolation of receptor proteins that bind the plant hormone abscisic acid (ABA). The structural features required for biological activity have been preserved, and the probe has been demonstrated to bind to known ABA-binding proteins.
Nyangulu
James M
JM
Plant Biotechnology Institute, National Research Council of Canada, 110 Gymnasium Place, Saskatoon, Saskatchewan S7N 0W9, Canada.
Galka
Marek M
MM
Jadhav
Ashok
A
Gai
Yuanzhu
Y
Graham
Cindy M
CM
Nelson
Ken M
KM
Cutler
Adrian J
AJ
Taylor
David C
DC
Banowetz
Gary M
GM
Abrams
Suzanne R
SR
D000040:Abscisic Acid / Q000031:analogs & derivatives / Q000378:metabolism*; D000595:Amino Acid Sequence; D001937:Brassica / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000032:analysis / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010940:Plant Proteins; D011956:Receptors, Cell Surface; D000040:Abscisic Acid; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C107203:abscisic acid 8'-hydroxylase