TY - JOUR
T1 - Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins
AU - Matsui, Taei
AU - Kihara, Chisato
AU - Fujimura, Yoshihiro
AU - Mizuochi, Tsuguo
AU - Titani, Koiti
N1 - Funding Information:
We are grateful to Mr. Masami Suzuki for excellent technical assistance and to Ms. Atsuko Nagata for typing the manuscript. This work was supported in part by Grants-in-Aid from the Fujita Health University and from the Ministry of Education, Science and Culture of Japan for Scientific Research on Priority Areas (to K.T.).
PY - 1991/8/15
Y1 - 1991/8/15
N2 - Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins. The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment. These reactivities were consistent with the major oligosaccharide structure reported except for UEA-I. The reactivity with UEA-I was greatly decreased after digestion of the protein with either α-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation. vWF and UEA-I have been independently used as a good marker for human endothelial cells. Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
AB - Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins. The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment. These reactivities were consistent with the major oligosaccharide structure reported except for UEA-I. The reactivity with UEA-I was greatly decreased after digestion of the protein with either α-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation. vWF and UEA-I have been independently used as a good marker for human endothelial cells. Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
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U2 - 10.1016/0006-291X(91)91028-B
DO - 10.1016/0006-291X(91)91028-B
M3 - Article
C2 - 1872845
AN - SCOPUS:0026069899
SN - 0006-291X
VL - 178
SP - 1253
EP - 1259
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -