Degradation of luteinizing hormone-releasing hormone (LHRH) by brain prolyl endopeptidase with release of des-glycinamide LHRH and glycinamide.
A highly purified preparation of rabbit brain prolyl endopeptidase cleaved the decapeptide luteinizing hormone-releasing hormone (LHRH) at the ProGly . NH2 bond leading to the release within 1-3 h incubation at 37 degrees C of des-glycinamide LHRH and glycinamide. Evidence for this site of cleavage was obtained by the detection of glycinamide or glycine and groups by a microdanyslation procedure, and by separation of the breakdown products by high performance liquid chromatography (HPLC) on a revers phase C-18 column. Incubation led to the appearance of two new peaks as detected by HPLC one of which was collected and shown to have the composition consistent with des-glycinamide LHRH. The other peak ran in the position identical to that of authentic glycinamide. Results suggest that prolyl endopeptidase could play a role in the inactivation of LHRH in vivo.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D010450:Endopeptidases / Q000378:metabolism*; D007987:Gonadotropin-Releasing Hormone / Q000378:metabolism*; D066298:In Vitro Techniques; D011817:Rabbits
D007987:Gonadotropin-Releasing Hormone; D010450:Endopeptidases