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Endocrinology, Vol 116, 353-358, Copyright © 1985 by Endocrine Society

ARTICLES

Secreted mouse prolactin (PRL) and stored ovine PRL. II. Role of amides in receptor binding and immunoreactivity

LS Haro and FJ Talamantes

Native PRL and des-amido forms 1, 2, and 3 were tested for their individual immunochemical and receptor-binding abilities. The results show that deamidation of either secreted mouse PRL or stored ovine PRL alters their binding in a radioreceptor assay. For each accumulated deamidation there was a statistically significant (P less than 0.05) decrease in the binding potency of either stored ovine PRL or secreted mouse PRL to a cell membrane receptor preparation. RIAs indicated that there was a statistically significant (P less than 0.05) decrease in PRL's immunopotency toward polyclonal antisera only when select residues deamidated. This study suggests that all the asn/gln residues which deamidate in order to make des-amido forms 1, 2, and 3 constitute part of the receptor-binding domains of both secreted and stored PRLs, while only a fraction of those same residues form portions of PRL's antigenic sites. Thus PRL's receptor-binding surface is separated from its antigenic sites, with only partial overlap being indicated. Our data also indicate that there are no major structural differences in the receptor-binding domains of secreted and stored PRLs. We also see that the receptor-binding domain of PRL has been highly conserved throughout evolution. Since the binding affinity of PRL to a membrane- bound receptor can be altered through deamidation, we view the process as a plausible regulatory mechanism for controlling the quantitative action of PRL at a given target organ.


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