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PMID: 4185494 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 113 ·No. 2 ·1969-06-00 ·Pages 299-305

Marchalonis JJ

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. 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.

MeSH Terms
Animals Centrifugation, Density Gradient Electrophoresis Humans Hydrogen Peroxide Immunoglobulin G Iodine Isotopes Macroglobulins Methods Peptides/analysis Peroxidases Rabbits Tyrosine/analysis gamma-Globulins
Chemicals
Immunoglobulin G Iodine Isotopes Macroglobulins Peptides gamma-Globulins Tyrosine Hydrogen Peroxide Peroxidases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Marchalonis J J
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22 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1130299
Published
1969-06-00
Pages
299-305
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1184636
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1130299 PMC Full Text View journal details
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