Department of Biochemistry, Fukushima Medical University, Fukushima, Japan.
Department of Human Life Science, Fukushima Medical University School of Nursing, Fukushima, Japan.
Methods Mol Biol. 2020;2132:165-171. doi: 10.1007/978-1-0716-0430-4_17.
Glycoforms are otherwise identical proteins with different glycosylation. A lectin, Sambucus sieboldiana agglutinin (SSA), specifically binds glycoforms having α2,6-sialyl residues. The binding is found to inhibit antigen-antibody reaction; e.g., SSA inhibits anti-transferrin antibody binding to α2,6-sialylated transferrin (Tf) (SSA inhibition). SSA inhibition is not observed with other Tf glycoforms, indicating that the inhibition is glycoform-specific. Here we describe the application of SSA inhibition to ELISA as a specific assay for quantifying α2,6-sialylated Tf.
糖型是指具有不同糖基化的相同蛋白质。凝集素，接骨木凝集素（SSA），特异性结合具有α2,6-唾液酸残基的糖型。已发现该结合抑制抗原-抗体反应；例如，SSA 抑制抗转铁蛋白抗体与α2,6-唾液酸化转铁蛋白（Tf）（SSA 抑制）的结合。其他 Tf 糖型不会观察到 SSA 抑制，表明抑制是糖型特异性的。本文描述了 SSA 抑制在 ELISA 中的应用，作为定量检测α2,6-唾液酸化 Tf 的特异性检测方法。
