Binding properties of protein Arp, a bacterial IgA-receptor
作者： Bo Åkerström , Annika Lindqvist , Gunnar Lindahl
DOI: 10.1016/0161-5890(91)90147-C
关键词: Biochemistry 、 Peptide 、 Antibody 、 Fragment crystallizable region 、 Cell surface receptor 、 Amino acid 、 Binding protein 、 Molecular biology 、 Biology 、 Receptor 、 Protein A/G
摘要: A cell surface receptor that binds to the Fc region of IgA is expressed by certain strains group streptococci. The physico-chemical properties and binding characteristics this receptor, called protein Arp, were studied. Like bacterial receptors bind IgG, Arp has an elongated shape no disulfide bonds. affinity constant for three different molecular forms was determined, found be more than ten-fold higher serum two complexed IgA: secretory bound alpha 1-microglobulin. Cleavage with CNBr resulted in a peptide corresponding located outside wall, except N-terminal 52 amino acids. This CNBr-fragment did not IgA, which strongly suggests IgA-binding part molecule. In addition also IgG weakly. pH-dependence these types different, maximal at neutral pH (5-7) acidic (3-5). Both shows strong specificity immunoglobulins human origin.
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