The complete amino acid sequence of prolactin from the bullfrog, Rana catesbeiana

Akikazu Yasuda, Kazuo Yamaguchi, Tetsuya Kobayashi, Kazutoshi Yamamoto, Sakae Kikuyama, Hiroshi Kawauchi*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    19 Citations (Scopus)


    The complete amino acid sequence of prolactin (PRL) from an amphibian species, the bullfrog (Rana catesbeiana), has been determined and conserved residues and domains were analyzed by sequence comparison of PRLs from 15 species of five major vertebrate classes. The bullfrog PRL consists of 197 amino acid residues with three disulfide linkages formed between residues 4-11, 58-172, and 189-197. The bullfrog PRL shows the highest identity with sea turtle PRL (75%); lower identities with chicken PRL (72%), pig, horse, and fin whale PRLs (68%), human, cattle, sheep, and elephant PRLs (60-58%), and rat and mouse PRLs (50%); and significantly lower identity with teleost PRLs (about 30%). It is apparent that all tetrapod PRLs characterized so far contain three disulfide bonds in homologous positions and differ from teleost PRLs which lack the N-terminal disulfide loop. The tetrapod and teleost PRLs share 34 common residues and these conserved residues are clustered in six domains (PD1 to PD6), suggesting that these common residues, or at least part of them, are responsible for the activities common to all PRLs. On the other hand, PD5 is conserved significantly within tetrapod PRLs, but to a lesser extent in teleos PRLs, suggesting that the PD5 contributes to the activities specific to tetrapod PRLs.

    Original languageEnglish
    Pages (from-to)218-226
    Number of pages9
    JournalGeneral and Comparative Endocrinology
    Issue number2
    Publication statusPublished - 1991

    ASJC Scopus subject areas

    • Endocrinology


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