Primary structure of common carp prolactins.

The complete amino acid sequence of common carp (Cyprinus carpio) prolactin (PRL) has been determined. One milligram of carp PRL was reduced, carboxymethylated, and then cleaved with cyanogen bromide and several enzymes. Another milligram of carp PRL was digested with lysyl endopeptidase. The resulting fragments were separated by reverse-phase high-performance liquid chromatography and subjected to sequence analysis by the automatic Edman method with a gas-liquid sequencer and the manual DNS-Edman method. The carp PRL consists of 186 amino acid residues with two disulfide linkages formed between residues 46-160 and 177-186. In addition, it lacks the linkage in the amino-terminal portion of mammalian prolactins, as do salmon and tilapia PRLs, and shows 77% sequence identity with salmon PRL and 36% identity with mammalian PRLs. The sequence comparison has been performed with 190 alignment positions. Four conserved segments of the alignment positions 1-32, 46-66, 71-94, and 155-182 that were found between salmon and mammalian PRLs are further confirmed in carp PRL. Variant residues are clustered in the region of residues 98-143 which has 48% sequence identity with salmon PRL and only 2% with mammalian PRL.