TY - JOUR
T1 - Defining carbohydrate specificity of Ricinus communis agglutinin as Ga1 β 1 → 4GlcNAc (II) > Gal β 1 → 3GlcNAc (I) > Gal α 1 → 3Gal (B) > Gal β 1 → 3GalNAc (T)
AU - Wu, June H.
AU - Herp, Anthony
AU - Wu, Albert M.
PY - 1993/3
Y1 - 1993/3
N2 - To define carbohydrate specificity of Ricinus communis agglutinin (RCA1), the combining site of RCA1 was further characterized by quantitative precipitin (QPA) and precipitin-inhibition assays (QPIA). Among the oligosaccharides tested for QPIA, Gal β 1 → 4GlcNAc (II, human blood group type II precursor sequence) was found to be 7.1 times more active than Gal β 1 → 3GalNAc (T, Thomsen-Friedenreich sequence) and about 1.7 times more active than the other three disaccharides tested - Gal β 1 → 4Man, Gal β 1 → 3dAra and Gal β 1 → 6GalNAc. Gal α 1 → 4Gal, the receptor of the uropathogenic E. coli ligand was 3.6 times less active than the II sequence. These results indicate that the β 1 →4 linkage of the terminal Gal to subterminal GlcNAc is important as this β 1 → 4GlcNAc sequence is at least 1.6 times more active than other types of disaccharides. Among the glycoproteins examined for QPA, native and desialized bovine submandibular glycoproteins, native and desialized human plasma α1-acid glycoproteins, as well as crude hog stomach mucin and its three mild acid hydrolyzed products reacted well with the lectin. These glycoproteins precipitated over 75% of the lectin nitrogen added indicating that RCA1 has the ability to recognize Gal β 1 → 4 3GlcNAc and/or the related residues at the non-reducing ends and at positions in the interior of the chains. However, Tn (GalNAc α 1 → Ser/Thr sequence) rich glycoproteins such as desialized ovine submandibular glycoprotein and desialized armadillo salivary glycoprotein, in which over 90% of the carbohydrate side chains are Tn determinants with none or only a trace of I/II or T determinants, precipitated poorly with RCA1. From the present and previous results obtained, the carbohydrate specificity of RCA1 can be constructed and summarized in decreasing order by lectin determinants as follows: II (Gal β 1 → 4GlcNAc) > I (Gal β 1 → 3GlcNAc) > E (Gal α 1 → 4Gal) and B (Gal α 1 → 3Gal) > T (Gal β 1 → 3GalNAc), while Tn (GalNAc α 1 → Ser/Thr) is a poor inhibitor.
AB - To define carbohydrate specificity of Ricinus communis agglutinin (RCA1), the combining site of RCA1 was further characterized by quantitative precipitin (QPA) and precipitin-inhibition assays (QPIA). Among the oligosaccharides tested for QPIA, Gal β 1 → 4GlcNAc (II, human blood group type II precursor sequence) was found to be 7.1 times more active than Gal β 1 → 3GalNAc (T, Thomsen-Friedenreich sequence) and about 1.7 times more active than the other three disaccharides tested - Gal β 1 → 4Man, Gal β 1 → 3dAra and Gal β 1 → 6GalNAc. Gal α 1 → 4Gal, the receptor of the uropathogenic E. coli ligand was 3.6 times less active than the II sequence. These results indicate that the β 1 →4 linkage of the terminal Gal to subterminal GlcNAc is important as this β 1 → 4GlcNAc sequence is at least 1.6 times more active than other types of disaccharides. Among the glycoproteins examined for QPA, native and desialized bovine submandibular glycoproteins, native and desialized human plasma α1-acid glycoproteins, as well as crude hog stomach mucin and its three mild acid hydrolyzed products reacted well with the lectin. These glycoproteins precipitated over 75% of the lectin nitrogen added indicating that RCA1 has the ability to recognize Gal β 1 → 4 3GlcNAc and/or the related residues at the non-reducing ends and at positions in the interior of the chains. However, Tn (GalNAc α 1 → Ser/Thr sequence) rich glycoproteins such as desialized ovine submandibular glycoprotein and desialized armadillo salivary glycoprotein, in which over 90% of the carbohydrate side chains are Tn determinants with none or only a trace of I/II or T determinants, precipitated poorly with RCA1. From the present and previous results obtained, the carbohydrate specificity of RCA1 can be constructed and summarized in decreasing order by lectin determinants as follows: II (Gal β 1 → 4GlcNAc) > I (Gal β 1 → 3GlcNAc) > E (Gal α 1 → 4Gal) and B (Gal α 1 → 3Gal) > T (Gal β 1 → 3GalNAc), while Tn (GalNAc α 1 → Ser/Thr) is a poor inhibitor.
UR - http://www.scopus.com/inward/record.url?scp=0027528908&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(93)90062-G
DO - 10.1016/0161-5890(93)90062-G
M3 - 文章
C2 - 7681148
AN - SCOPUS:0027528908
SN - 0161-5890
VL - 30
SP - 333
EP - 339
JO - Molecular Immunology
JF - Molecular Immunology
IS - 4
ER -