Proceedings of the National Academy of Sciences · 1990 · 188 citations · 17 references
Life SciencesBiochemistryMolecular BiologyGene ExpressionHormone BiochemistryNeuroendocrinologyGrowth HormonePituitary Gland FunctionPituitary HormonesProteolytic ProcessingAmino AcidsCdna CloningCdna SynthesisCloningComplementary Dna (Cdna) CloningPituitary Hormone BiochemistryPituitary Peptide HormonesSignal Peptide Analysis
From a flounder pituitary cDNA library, cDNA clones encoding a 28-kDa glycoprotein produced by the pars intermedia of the pituitary were isolated and characterized. Nucleotide sequencing demonstrated a precursor of the 28-kDa protein, which consisted of 231 amino acid residues, to be cleaved into a signal peptide (24 amino acids) and a mature protein (207 amino acids) containing one N-glycosylation site. By comparison of amino acid sequences, the 28-kDa protein was found to be distantly and similarly related to growth hormone and prolactin. Consequently, it was named somatolactin. Somatolactin mRNAs were specifically expressed as 1.2 and 1.8 kb poly(A)+ RNAs in flounder pituitary.
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