The effects of various chemical and enzymatic treatments on the biological activity of porcine luteinizing hormone-releasing hormone (LH-RH) are described. This experiment was performed before the elucidation of the structure of LH-RH. LH-RH activity was abolished by the following endopeptidases: chymotrypsin, subtilisin, papain, and thermolysin, but not by pepsin or trypsin. Exopeptidases did not affect LH-RH activity, but a purified preparation of pyrolidone carbosylpeptidase did. The amino acid sequence of LH-RH/FSH-RH was established to be (pyro)Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-Amine. This decapeptide lacks both the Amine terminus and the COOH terminus. Its Amine-terminal dipeptide sequence,(pyro)Glu-His, is similar to that of tyrotropin-releasing hormone. The lack of inactivation by the exopeptidases is in good agreement with these findings. Treatment with various chemical reagents showed that tyrosine, histidine, tryptophan, and arginine in LH-RH are important for its biological activity. Nitrous acid and Edman degradation did not inactivate LH-RH. These results are also in agreement with the determined structure of LH-RH. This hormone showed a high follicle-stimulating hormone-releasing hormone (FSH-RH) activity. The inactivation of LH-RH was always accompanied by a loss of FSH-RH activity. These experiments also shed some light on the structure-activity relationship of this hormone.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|State||Published - Dec 25 1971|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology