Isolation of a melibiose-binding protein from human spleen.
A melibiose-binding protein was isolated from human spleen by serial affinity chromatography on lactose-, mannose-, and melibiose-Sepharose. The purified protein agglutinated rabbit erythrocytes and re-bound to melibiose, but did not bind to murine nor human laminin. The protein was composed of approximately 58 kDa and 26 kDa polypeptides. The polypeptides were detected in buffy coat cell extracts and they were synthesized in vitro by B lymphoblastoid cells. The polypeptides did not react with anti-galaptin, anti-C-reactive protein, anti-amyloid P, anti-keratin, and anti-rat lung lectin 29 sera. The 58 kDa polypeptide reacted very weakly with anti-core-specific lectin serum and reacted with anti-IgG serum. The data suggest that the major protein isolated is an anti-Ga1 alpha 1-->6 immunoglobulin.
Sharma
A
A
Department of Gynecologic Oncology, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
Ahmed
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H
Allen
H J
HJ
D000818:Animals; D015153:Blotting, Western; D002352:Carrier Proteins / Q000302:isolation & purification*; D005697:Galactosides / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D037102:Lectins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism*; D008553:Melibiose / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D011817:Rabbits; D013154:Spleen / Q000737:chemistry*
D002352:Carrier Proteins; D005697:Galactosides; D037102:Lectins; D008553:Melibiose