DOI: 10.1042/bj1130299. An enzymic method for the trace iodination of immunoglobulins and other proteins

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

10.1042/bj1130299

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

Abstract

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. γG immunoglobulin that had been labelled to a specific radioactivity of 5μc/μg. by use of carrier-free [125I]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 [125I]iodide was bound to tyrosyl residues. 4. Proteins differ in their susceptibility to iodination by this method. Human γG immunoglobulin, for example, is iodinated more than ten times as readily as is human α2-macroglobulin under the same conditions. 5. Lactoperoxidase catalyses the iodination of proteins much more readily than does horseradish peroxidase.

Bibliography

Marchalonis, J. J. (1969). An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochemical Journal, 113(2), 299â305.

Authors 1

J. J. Marchalonis (first)

References 0 Referenced 1,026

None

Dates

Type	When
Created	10 years ago (Aug. 13, 2015, 5:37 p.m.)
Deposited	3 years, 8 months ago (Nov. 29, 2021, 4:23 p.m.)
Indexed	3 weeks, 2 days ago (Aug. 2, 2025, 12:08 a.m.)
Issued	56 years, 2 months ago (June 1, 1969)
Published	56 years, 2 months ago (June 1, 1969)
Published Print	56 years, 2 months ago (June 1, 1969)

Funders 0

None

BibTeX

@article{Marchalonis_1969, title={An enzymic method for the trace iodination of immunoglobulins and other proteins}, volume={113}, ISSN={0306-3283}, url={http://dx.doi.org/10.1042/bj1130299}, DOI={10.1042/bj1130299}, number={2}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Marchalonis, J. J.}, year={1969}, month=jun, pages={299–305} }

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  "abstract": "<jats:p>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. \u03b3G immunoglobulin that had been labelled to a specific radioactivity of 5\u03bcc/\u03bcg. by use of carrier-free [125I]iodide gave no evidence of denaturation when analysed by electrophoresis and density-gradient ultracentrifugation. 3. Tryptic hydrolysis and peptide \u2018mapping\u2019 of a completely characterized peptide radioiodinated by this method showed that the [125I]iodide was bound to tyrosyl residues. 4. Proteins differ in their susceptibility to iodination by this method. Human \u03b3G immunoglobulin, for example, is iodinated more than ten times as readily as is human \u03b12-macroglobulin under the same conditions. 5. Lactoperoxidase catalyses the iodination of proteins much more readily than does horseradish peroxidase.</jats:p>",
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