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Differential binding of human blood group Sd(a+) and Sd(a−) Tamm‐Horsfall glycoproteins with Dolichos biflorus and Vicia villosa ‐B 4 agglutinins
Author(s) -
Wu Albert M.,
Wu June H.,
Watkins Winifred M.,
Chen Chie-Pein,
Song Shuh-Chyung,
Chen Yuen-Yuen
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00617-6
Subject(s) - dolichos , glycoprotein , villosa , chemistry , vicia villosa , biology , biochemistry , botany , cover crop , agronomy
The binding patterns of human blood group Sd(a+) and Sd(a−) Tamm‐Horsfall glycoproteins (THGPs) with respect to four GalNAc specific agglutinins were studied by quantitative precipitin assay (QPA) and enzyme linked lectinosorbent assay (ELLSA). Of the native and asialo Sd(a+) and Sd(a−) THGP tested by QPA and ELLSA, only native and asialo Sd(a+) bound well with Dolichos biflorus (DBA) and Vicia villosa ‐B 4 (VVA‐B 4 ), while Sd(a−) THGP reacted poorly with these two lectins. Neither Sd(a+) nor Sd(a−) THGPs reacted with two other GalNAc α‐anomer specific lectins: Codium fragile subspecies tomentosoides and Artocarpus integrifolia . Furthermore, the binding of asialo Sd(a+)THGP‐VVA‐B 4 and native Sd(a+)THGP‐DBA through GalNAcβ→ was confirmed by inhibition assay. These results demonstrate that DBA and VVA‐B 4 are useful reagents to differentiate between Sd(a+) and Sd(a−) THGP.