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Studies on the structural and conformational basis for the relative resistance of serum and secretory immunoglobulin A to proteolysis


, : Studies on the structural and conformational basis for the relative resistance of serum and secretory immunoglobulin A to proteolysis. Journal of Immunology 112(3): 949-959

Both human colostral IgA (prepared as described in DSA 35, 3582) and serum IgA were more resistant to proteolysis than was serum IgG. IgA myeloma dimer was broken down to a monomer-like fragment after incubation for 3 h with Pronase whilst colostral IgA dimer remained intact. Colostral IgA dimer required a greater concn. (35mM) of dithiothreitol than did normal serum IgA and IgA myeloma dimer (10mM) to convert it to a form which was susceptible to proteolysis.

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PMID: 4855821


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