| Literature DB >> 3379064 |
K Yamaguchi1, J L Specker, D S King, Y Yokoo, R S Nishioka, T Hirano, H A Bern.
Abstract
The complete amino acid sequences of a pair of tilapia (Oreochromis mossambicus) prolactins (PRLs) were determined. The larger PRL of molecular mass 20,836 Da consists of 188 amino acid residues. The smaller PRL of molecular mass 19,584 Da is 11 residues shorter. On alignment of the two sequences, the 19.6-kDa PRL (tPRL177) has two conspicuous deletions on the NH2-terminal side of the disulfide bond which connects the first and second cysteine residues. The degree of similarity between the two PRL sequences is unexpectedly low (130 identical residues, 69%) compared with that between the variants of other teleostean PRLs. Circular dichroism spectra and hydropathy profiles suggest structural similarity of the two PRLs. The sequence of the 20.8-kDa PRL (tPRL188) has 69% identity with that of salmon PRL. The sequence of tPRL177 is 56% identical with that of salmon PRL. Each tilapia PRL is equally similar to mammalian PRLs (about 30% identical residues). Regions highly conserved among teleostean and mammalian PRLs were identified on the COOH-terminal side of the disulfide bond connecting the first and second cysteine residues.Entities:
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Year: 1988 PMID： 3379064
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157