Affinity purification and characterization of recombinant human galectin-1.
Galectin-1, a polypeptidic factor that can have major effects on cell growth and apoptosis, was overexpressed in E. coli. This protein was purified to homogeneity by affinity chromatography on lactose coupled to divinylsulfone-activated agarose. The recombinant galectin-1 (rGAL1) was compared with the homologous protein purified from human brain tissue using two-dimensional electrophoresis on immobilized pH gradient (IPG-DALT). rGAL1 had a major isoelectric point of 5.4 (major pI of tissular galectin-1, 5.1) and its subunit molecular mass was 14500. Addition of rGAL1 to Jurkat T-lymphoblastoid cells induced cell death in a concentration-dependent manner.
Fouillit
M
M
Biochimie Cellulaire des Hémopathies Lymphoïdes, UFR SMBH-Léonard de Vinci, Université Paris Nord, Bobigny, France.
Lévi-Strauss
M
M
Giudicelli
V
V
Lutomski
D
D
Bladier
D
D
Caron
M
M
Joubert-Caron
R
R
D001923:Brain Chemistry; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D037483:Galectin 1; D015870:Gene Expression; D006388:Hemagglutinins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D007526:Isoelectric Point; D037102:Lectins; D011994:Recombinant Proteins
D037483:Galectin 1; D006388:Hemagglutinins; D037102:Lectins; D011994:Recombinant Proteins