Abstract:
:The immunoglobulin E-binding protein, epsilon BP (also known as CBP35, Mac-2, L-34, and L-29), is a beta-galactoside-binding protein of approximately 30 kDa and a member of the animal lectin family termed S-type or S-Lac. Multiple biological activities have been attributed to this lectin such as mediation of IgE binding to the surface of Langerhans cells and activation of mast cells through binding to the high affinity IgE receptor. In order to better understand the cell-binding activity and the proposed role for epsilon BP as a biological response modifier, we have studied the specificity of binding of the radioiodinated epsilon BP to a series of lipid-linked, structurally defined oligosaccharide sequences of the lacto/neolacto family. The results show that the minimum lipid-linked oligosaccharides that can support epsilon BP binding are pentasaccharides of the lacto/neolacto series and that the lectin binds more strongly to oligosaccharides of this family that bear the blood group A, B, or B-like determinants than to those bearing blood group H. This preferential binding of epsilon BP is also manifest with whole cells, as erythrocytes of blood groups A and B are more strongly bound by epsilon BP than those of blood group O. Blood group Le(a) and Le(x) sequences are not bound by the lectin.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Biochemistryjournal_title
Biochemistryauthors
Feizi T,Solomon JC,Yuen CT,Jeng KC,Frigeri LG,Hsu DK,Liu FTdoi
10.1021/bi00186a038subject
Has Abstractpub_date
1994-05-24 00:00:00pages
6342-9issue
20eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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