Synthesis of a biospecific adsorbent for the purification of the three human retinoic acid receptors by affinity chromatography.
The total synthesis of an affinity gel suitable for the purification of retinoic acid receptors (hRARs) is reported. A chalcone derived from a potent retinobenzoic acid (Ch55) was chosen as the ligand and fixed to an immobilized matrix by coupling with the N-hydroxysuccinimide ester of agarose (Affi-Gel 10, Bio-Rad Laboratories). Efficiencies of purification of the different human RARs were tested, using recombinant receptors produced with the baculovirus expression system.
Bourguet
W
W
Unité 16 INSERM, Laboratoire de Biochimie des Protéines, Lille, France.
Sablonnière
B
B
Formstecher
P
P
Chen
J Y
JY
Bernier
J L
JL
Hénichart
J P
JP
D002352:Carrier Proteins / Q000302:isolation & purification*; D002599:Chalcone / Q000031:analogs & derivatives* / Q000737:chemistry; D047188:Chalcones; D002846:Chromatography, Affinity; D006801:Humans; D015394:Molecular Structure; D018168:Receptors, Retinoic Acid; D011994:Recombinant Proteins / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives / Q000737:chemistry
D002352:Carrier Proteins; D047188:Chalcones; D018168:Receptors, Retinoic Acid; D011994:Recombinant Proteins; D002599:Chalcone; C032392:Affi-Gel 10; D012685:Sepharose; C054189:3,5-di-tert-butylchalcone 4'-carboxylic acid