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Science 11 April 1980:
Vol. 208. no. 4440, pp. 183 - 185
DOI: 10.1126/science.6244620
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Articles

Science, Vol 208, Issue 4440, 183-185
Copyright © 1980 by American Association for the Advancement of Science

articles

High-molecular-weight immunoreactive beta-endorphin in extracts of human placenta is a fragment of immunoglobulin G

JH Julliard, T Shibasaki, N Ling, and R Guillemin

A high-molecular-weight protein with beta-endorphin- and adrenocorticotropin-immunoreactivities was isolated from extracts of human placenta after several purification steps, including immunoadsorption with a well-characterized antiserum raised to beta-endorphin. This protein was identified as the heavy chain of the human immunoglobulin class IgG1. These results have led to the recognition of homologies in the amino acid sequences of these physiologically unrelated molecules. They also suggest caution in accepting immunological competence as the sole criterion of the chemical identity of a ligand.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Models for the deposition of Mesozoic-Cenozoic fine-grained organic-carbon-rich sediment in the deep sea.
M. A. Arthur, W. E. Dean, and D. A. V. Stow (1984)
Geological Society, London, Special Publications 15, 527-560
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Science. ISSN 0036-8075 (print), 1095-9203 (online)