Isolation and structural characterization of chicken hypothalamic luteinizing hormone releasing hormone

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Abstract
Studies on partially purified chicken hypothalamic luteinizing hormone releasing hormone (LHRH) utilizing chromatography, radioimmunoassay with region‐specific antisera, enzymic inactivation, and chemical modification established that the peptide is structurally different from mammalian hypothalamic LHRH. These studies demonstrated that arginine in position 8 is substituted by a neutral amino acid. On the basis of conformational criteria and evolutionary probability of amino acid interchange for arginine, the most likely substitution was glutamine. We therefore synthesized [Gln8]‐LHRH and established that it had identical chromatographic, immunologic, and biological properties to the natural chicken peptide. In concurrent studies, purification of 17 μg of an LHRH from 249,000 chicken hypothalami was achieved using acetic acid extraction, immuno‐affinity chromatography, and cation exchange and reverse phase high performance liquid chromatography. Amino acid composition and sequence analyses confirmed the structure of this form of chicken LHRH as pGlu‐His‐Trp‐Ser‐Tyr‐Gly‐Leu‐Gln‐Pro‐Gly‐NH2.