Abstract
The complete amino acid sequence of prolactin (PRL) from a reptile, the sea turtle ( Chelonia mydas), was determined for the first time. Sequence analysis was performed on fragments obtained from cleavage of intact and performic acid-oxidized hormone with lysyl endopeptidase, Staphylococcus aureus protease, and o-iodosobenzoic acid employing manual Edman degradation. The sea turtle PRL consists of 198 amino acid residues with three disulfide linkages formed between residues 4–11, 58–173, and 190–198 and possesses heterogeneity indicated by four replacements at positions 55, 145, 148, and 171. Sequence comparison with other vertebrate PRLs revealed that the degree of sequence identity conforms well to expectations based on phylogeny except for the rodent PRLs; sea turtle PRL has 86% identity with chicken PRL; 81% with horse, pig, and fin whale PRLs; 75-71% with cattle, sheep, and human PRLs; 60-56% with mouse and rat PRLs; and 35-31% with carp, salmon, and tilapia PRLs.
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