Affinity purification and characterization of recombinant human galectin-1

被引：21

作者：

Fouillit, M

Lévi-Strauss, M

Giudicelli, V

Lutomski, D

Bladier, D

Caron, M

Joubert-Caron, R

机构：

[1] Univ Paris Nord, UFR SMBH Leonard de Vinci, F-93017 Bobigny, France

[2] Hop Necker Enfants Malad, INSERM U25, Immunol Clin, F-75743 Paris 15, France

来源：

JOURNAL OF CHROMATOGRAPHY B | 1998年 / 706卷 / 01期

关键词：

polypeptides; galectin-1;

D O I：

10.1016/S0378-4347(97)00336-8

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 14 500. Addition of rGAL1 to Jurkat T-lymphoblastoid cells induced cell death in a concentration-dependent manner. (C) 1998 Elsevier Science B.V.

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页码：167 / 171

页数：5

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