TY - JOUR
T1 - Fraction A of armadillo submandibular glycoprotein and its desialylated product as sialyl-Tn and Tn receptors for lectins
AU - Wu, Albert M.
AU - Shen, F. shiun
AU - Herp, Anthony
AU - Song, Shuh Chyung
AU - Wu, June H.
PY - 1995/2/27
Y1 - 1995/2/27
N2 - Fraction A of the armadillo submandibular glycoprotein (ASG-A) is one of the simplest glycoproteins among mammalian salivary mucins. The carbohydrate side chains of this mucous glycoprotein have one-third of the NeuAcα2→6GalNAc (sialyl-Tn) sequence and two thirds of Tn (GalNAcα→Ser/Thr) residues. Those of the desialylated product (ASG-Tn) are almost exclusively unsubstituted GalNAc residues (Tn determinant). When the binding properties of these glycoproteins were tested by a precipitin assay with Gal, GalNAc and GlcNAc specific lectins, it was found that ASG-Tn reacted strongly with all of the Tn-active lectins and completely precipitated Vicia villosa (VVL both B4 and mixture of A and B), Maclura pomifera (MPA), and Artocarpus integrifolia (jacalin) lectins. However, it precipitated poorly or negligibly with Ricinus communis (RCA1); Dolichos biflorus (DBA); Viscum album, ML-1; Arachis hypogaea (PNA), and Triticum vulgaris (WGA). The reactivity of ASG-A (sialyl-Tn) was as active as that of ASG-Tn with MPA and less or slightly less active than that of ASG-Tn with VVL-A+B, VVLB4, HPA, WFA, and jacalin, as one-third of its Tn was sialylated. These findings indicate that ASG-A and its desialylated product (ASG-Tn) are highly useful reagents for the differentiation of Tn, T (Galβ1→3GalNAc), A (GalNAcα1→3Gal) or Gal specific lectins and monoclonal antibodies against such epitopes.
AB - Fraction A of the armadillo submandibular glycoprotein (ASG-A) is one of the simplest glycoproteins among mammalian salivary mucins. The carbohydrate side chains of this mucous glycoprotein have one-third of the NeuAcα2→6GalNAc (sialyl-Tn) sequence and two thirds of Tn (GalNAcα→Ser/Thr) residues. Those of the desialylated product (ASG-Tn) are almost exclusively unsubstituted GalNAc residues (Tn determinant). When the binding properties of these glycoproteins were tested by a precipitin assay with Gal, GalNAc and GlcNAc specific lectins, it was found that ASG-Tn reacted strongly with all of the Tn-active lectins and completely precipitated Vicia villosa (VVL both B4 and mixture of A and B), Maclura pomifera (MPA), and Artocarpus integrifolia (jacalin) lectins. However, it precipitated poorly or negligibly with Ricinus communis (RCA1); Dolichos biflorus (DBA); Viscum album, ML-1; Arachis hypogaea (PNA), and Triticum vulgaris (WGA). The reactivity of ASG-A (sialyl-Tn) was as active as that of ASG-Tn with MPA and less or slightly less active than that of ASG-Tn with VVL-A+B, VVLB4, HPA, WFA, and jacalin, as one-third of its Tn was sialylated. These findings indicate that ASG-A and its desialylated product (ASG-Tn) are highly useful reagents for the differentiation of Tn, T (Galβ1→3GalNAc), A (GalNAcα1→3Gal) or Gal specific lectins and monoclonal antibodies against such epitopes.
KW - Armadillo submandibular glycoprotein
KW - Lectin reactivity
UR - http://www.scopus.com/inward/record.url?scp=0028950399&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(95)00106-J
DO - 10.1016/0014-5793(95)00106-J
M3 - 文章
C2 - 7875333
AN - SCOPUS:0028950399
SN - 0014-5793
VL - 360
SP - 211
EP - 215
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -