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Horm Metab Res 1978; 10(6): 525-527
DOI: 10.1055/s-0028-1093384
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© Georg Thieme Verlag KG Stuttgart · New York

Analysis of Hog Thyroglobulin. Identification of Galactosamine and Absence of Lysinoalanine, a Potential Product of Tyrosine Coupling

A. E. Burkhardt [1] , M.  Wilchek [2] , J. E. Rall
  • Clinical Endocrinology Branch, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland, U.S.A.
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Publication History

Publication Date:
23 December 2008 (online)

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Abstract

A small peak in the amino acid analysis of hog thyroglobulin was observed in the region reported for lysinoalanine and galactosamine. Since galactosamine had been previously reported absent in hog thyroglobulin, the possibility that this peak was lysinoalanine, a potential product of the coupling of two iodotyrosines, was investigated. Tests, however, showed that the material was galactosamine and that hog thyroglobulin contains no significant amount of lysinoalanine. Approximately 5 moles of galactosamine were found per mole of thyroglobulin.

Key words

Thyroglobulin - Galactosamine - Lysinoalanine

1 Present address, Ames Division, Miles Laboratories, Inc., Elkhart, Indiana

2 Present address, Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel