An enzymic method for the trace iodination of immunoglobulins and other proteins.

نویسنده

  • J J Marchalonis
چکیده

1. A method is described for the trace iodination of immunoglobulins and other serum proteins by a system consisting of lactoperoxidase, hydrogen peroxide and iodide. 2. gammaG immunoglobulin that had been labelled to a specific radioactivity of 5muc/mug. by use of carrier-free [(125)I]iodide gave no evidence of denaturation when analysed by electrophoresis and density-gradient ultracentrifugation. 3. Tryptic hydrolysis and peptide ;mapping' of a completely characterized peptide radioiodinated by this method showed that the [(125)I]iodide was bound to tyrosyl residues. 4. Proteins differ in their susceptibility to iodination by this method. Human gammaG immunoglobulin, for example, is iodinated more than ten times as readily as is human alpha(2)-macroglobulin under the same conditions. 5. Lactoperoxidase catalyses the iodination of proteins much more readily than does horseradish peroxidase.

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Marchalonis J J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochemical J. 113:299-305, 1969

"After obtaining my PhD in biochemistry with CM. Edelman, I went to the laboratory of G.J.V. Nossal at the Walter and Eliza Hall Institute as a postdoctoral fellow to learn cellular immunology. At the time I joined the laboratory, Nossal and G.L. Ada were carrying out a series of studies using radioiodinated protein antigens designed to ascertain the distribution of antigen in lymphoid tissues ...

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عنوان ژورنال:
  • The Biochemical journal

دوره 113 2  شماره 

صفحات  -

تاریخ انتشار 1969