Interaction of a human blood group Sd(a−) Tamm‐Horsfall glycoprotein with applied lectins

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Abstract
Unlike the human blood group Sd(a+) Tamm‐Horsfall glycoprotein (THGP), the Sd(a−) one lacks terminal GalNAcβ1 → residues at the nonreducing ends. The binding properties of this glycoprotein and its asialo product with lectins were characterized by quantitative precipitin (QPA) and precipitin inhibition assays. Among 20 lectins tested by QPA, both native and asialo Sd(a−) THGP reacted best with Abrus precatorius and Ricinus communis and completely precipitated the lectin added. They also precipitated well Wistaria floribunda (WFA), Glycine max (SBA), Bauhinia purpurea alba, abrin‐a and ricin, all of which recognize the Galβ1 → 4GlcNacβ1 → sequence, although at different strength. The lectin‐glycan interactions were inhibited by Galβ1 → 4GlcNAc and Galβ1 → 4Glc. When the precipitability of Sd(a−) THGP was compared with that of the Sd(a+) phenotype, the native Sd(a−) THGP exhibited a 40% lesser affinity for WFA, SBA, WGA and mistletoe lectin‐I (ML‐I). Mapping the precipitation and inhibition profiles of the present study and the results of THGP Sd(a+), it is concluded that Sd(a−) THGP showed a strongly diminished affinity for GalNAcβ1 → active lectins (SBA and WFA) than the Sd(a+) phenotype.