TY - JOUR
T1 - Oligoclonal β-galactoside-binding immunoglobulins antigenically related to 14kda lectin in human serum and cerebrospinal fluid
T2 - Purification and characterization
AU - Joubert-Caron, Raymonde
AU - Caron, Michel
AU - Bochet, Pascal
AU - Chadli, Ahmed
AU - Delaporte, Pierre
AU - Schuller, Edmond
AU - Bladier, Dominique
N1 - Funding Information:
Acknowledgements-We thank S. H. Barondes and H. J. Gabius for antibodies against 14 kDa lectin from rat lung and bovine heart, R. Oriol for immobilized synthetic oligisaccharides and J. Koucourek for the lactosyl-based copolymer. We are grateful to Agnes Poulaud for his excellent photographic work and to Ctline Picaud for his help in affinity support preparation. This work was supported by grants from the INSERM (No. 896001) from the Delegation a la Recherche Clinique de I’Assistance Publique (No. 90012 and 91-04-05), from the Ministere de I’Education Nationale, Direction de la Recherche et des Etudes Doctorates (DRED), from the Association pour la Recherche sur la Sclerose en Plaques (ARSEP) and from Fondation de France.
PY - 1994/6
Y1 - 1994/6
N2 - 1. 1. An antiserum raised against a 14kDa β-galactoside specific lectin from human brain (HBL14) was used to probe blots from samples of serum and cerebrospinal fluid. The only HBL14-immunoreactive material detected was heavy and light chains of a β-galactoside-binding IgG fraction (lectin-like IgG). 2. 2. Lectin-like IgG, as well as IgG Fab fragments, compete with HBL14 for binding either to anti-HBL14 antibody or to a lactosyl polyacrylamide-based copolymer. 3. 3. Purification of lectin-like IgG was obtained by affinity chromatography on immobilized rabbit anti-lectin immunoglobulins. The carbohydrate-binding specificity of the purified molecules was restricted to β-Gal-containing structures and close to the HBL14 one.
AB - 1. 1. An antiserum raised against a 14kDa β-galactoside specific lectin from human brain (HBL14) was used to probe blots from samples of serum and cerebrospinal fluid. The only HBL14-immunoreactive material detected was heavy and light chains of a β-galactoside-binding IgG fraction (lectin-like IgG). 2. 2. Lectin-like IgG, as well as IgG Fab fragments, compete with HBL14 for binding either to anti-HBL14 antibody or to a lactosyl polyacrylamide-based copolymer. 3. 3. Purification of lectin-like IgG was obtained by affinity chromatography on immobilized rabbit anti-lectin immunoglobulins. The carbohydrate-binding specificity of the purified molecules was restricted to β-Gal-containing structures and close to the HBL14 one.
KW - Soluble lectin Immunoglobulins Affinity chromatography Anti-idiotypes
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U2 - 10.1016/0020-711X(94)90111-2
DO - 10.1016/0020-711X(94)90111-2
M3 - Article
C2 - 7520398
AN - SCOPUS:0028177249
SN - 0020-711X
VL - 26
SP - 813
EP - 823
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
IS - 6
ER -