关键词: Antigen-antibody reaction Cerebrospinal fluid Enzyme-linked immunosorbent assay Sambucus sieboldiana agglutinin Transferrin α2,6sialyl residue

Mesh : Antibodies / metabolism Antigen-Antibody Reactions / drug effects Blood Chemical Analysis Enzyme-Linked Immunosorbent Assay Glycosylation Humans N-Acetylneuraminic Acid / metabolism Plant Lectins / pharmacology Ribosome Inactivating Proteins / pharmacology Sambucus / metabolism Transferrin / analysis chemistry immunology

来  源:   DOI:10.1007/978-1-0716-0430-4_17

Abstract:
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.
摘要:
糖型在其他方面是具有不同糖基化的相同蛋白质。凝集素,Sambucussieboldiana凝集素(SSA),特异性结合具有α2,6-唾液酸残基的糖型。发现结合抑制抗原-抗体反应;例如,SSA抑制抗运铁蛋白抗体与α2,6-唾液酸化的运铁蛋白(Tf)的结合(SSA抑制)。其他Tf糖型未观察到SSA抑制,表明抑制是糖型特异性的。在这里,我们描述了SSA抑制在ELISA中的应用,作为定量α2,6-唾液酸化Tf的特异性测定。
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