Abstract
Active substances extracted from the Remak nerve of the chicken were subjected to chromatographic and electrophoretic separation followed by bioassay of contracting activities on the longitudinal muscle of the guinea-pig ileum (LMGPI) and on the isolated whole chick rectum (WCR). Gel filtration profiles on a Sephadex G-50 column showed two peaks of LMGPI-contracting activity and of WCR-contracting activity. No difference was seen in the enzymatic destruction between the LMGPI-contracting activity and substance P. Their similarities were also indicated by the parallelism of their elution curves in the gel chromatography on Sephadex G-25, their equal stability in acid solutions, and comparable antagonism and inhibition of the contractile effects on LMGPI by substance P antagonists and after desensitization of substance P receptors. Ion exchange chromatography revealed the existence of two main substances responsible for the LMGPI-contracting activity. One of them eluted at the same position as that for substance P, but differed in immunoreactivity and electrophoretic mobility from substance P. The WCR-contracting activity differed from the LMGPI-contracting activity in that it was pepsin-resistant and carboxypeptidase A-susceptible, and it eluted at a different position during ion exchange chromatography. It seems likely that the LMGPI-contracting activity in the extracts is attributed to a substance P-family of peptides, but the WCR-contracting activity is due to another substance of a peptide nature.
