Monoclonal Antibody to an Endogenous Neuropeptide with Putative Morphine-Modulating Activity

摘要

Monoclonal antibodies against phe-leu-phe-gln-pro-gln-arg-phe-NH2 (F-8-F-NH2), a FMRF-NH2-like peptide of bovine brain, have been produced and characterized. The antibodies showed varying degrees of cross-reactivity with peptides having arg-phe-NH2 at their C-termini but no cross-reactivity with met(5)-enkephalin-arg(6)-phe(7), NPY and PYY. The result suggests that these antibodies are directed to the C-terminal dipeptide, arg-phe-NH2, and the conformation of the peptide also contributes to the immunoreactive potency. The result also indicates the monoclonal antibodies are capable of differentiating-RH-NH2, the C-terminal dipeptide amide of FMRF-NH2-like peptides, from RY-NH2, the C-terminal dipeptide amide of NPY. An extract from bovine spinal cord was analyzed by HPLC coupled with RIA using the monoclonal antibodies. The major immunoreactivity was identified as F-8F-NH2 although there were some very small amounts of unidentified immunoreactive species. The specificity of these monoclonal antibodies is thus further confirmed and will be useful in differentiating the distribution of F-8-F-NH2 or mammalian FMRF-NH2-like peptides from that of NPY by immunohistochemical studies. (KT/AW)