Purification and characterization of luteinizing hormone-releasing hormone from codfish brain.
We have purified luteinizing hormone-releasing hormone (LH-RH) from codfish brain and have demonstrated its identity with salmon LH-RH (sLH-RH). An antiserum raised against sLH-RH was used in a specific radioimmunoassay (RIA) to monitor purification and to manufacture an immunoaffinity chromatography column for the initial purification step. The cross-reactivity of the sLH-RH RIA with mammalian LH-RH was 0.1%. Acid extracts of codfish brains were sequentially purified by immunoaffinity chromatography, gel-filtration chromatography, and three steps of reverse-phase HPLC. The purified material and synthetic sLH-RH coeluted on reverse-phase HPLC and exhibited similar biological activity in a dispersed pituitary cell bioassay. Furthermore, the amino acid composition of the purified material was identical to salmon LH-RH. These results suggest that there is structural conservation of LH-RH between these species of teleost fish.
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003429:Cross Reactions; D005399:Fishes / Q000502:physiology*; D007987:Gonadotropin-Releasing Hormone / Q000302:isolation & purification*; D011863:Radioimmunoassay; D013045:Species Specificity
D007987:Gonadotropin-Releasing Hormone