Purification of human galectin-1 produced in high-cell density cultures of recombinant Escherichia coli: a comparison with classic shake flask cultivation.
The aim of the present work was to develop a highly productive and simplified process for active human galectin-1 (Gal1) production. Gal1 is a beta-galactoside binding lectin that differentially affects biological and cellular functions such as immune surveillance and apoptosis. These effects have attracted the attention of researchers in cell biology, biochemistry and immunology. However, the production of sufficient amounts of recombinant human Gal1 (rhGal1) is needed to study of the effects of Gal1 during cell treatments. To this end, an high-yield expression of rhGal1 was achieved by high-cell density fed-batch cultivation using an exponential glycerol feeding strategy and rhGal1 was purified by a one-step purification scheme using affinity chromatography.
Lutomski
Didier
D
Laboratoire de Biochimie des Protéines et Protéomique, Immunopathologie et ImmunoIntervention (E.A. 3408), UFR SMBH Leonard de Vinci, Université Paris 13, 74 rue Marcel Cachin, Bobigny Cedex 93017, France. lutomski@smbh.univ-paris13.fr
Imam-Sghiouar
Naima
N
Blondeau
Karine
K
Caron
Michel
M
Joubert-Caron
Raymonde
R
D004926:Escherichia coli / Q000235:genetics; D037483:Galectin 1 / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification
D037483:Galectin 1; D011994:Recombinant Proteins