Gg. Turrigiano et al., PARTIAL-PURIFICATION, TISSUE DISTRIBUTION AND MODULATORY ACTIVITY OF A CRUSTACEAN CHOLECYSTOKININ-LIKE PEPTIDE, Journal of Experimental Biology, 187, 1994, pp. 181-200
Reversed-phase chromatography was used to separate several forms of ch
olecystokinin-like peptides (CCKLP) from the pericardial organs (PCOs)
of the spiny lobster Panulirus interruptus. Fast protein liquid chrom
atography of PCOs, stomatogastric ganglia (STGs) and eyestalks reveale
d five peaks of CCKLP (peaks A-E) that were common to all three tissue
s, as well as two additional peaks (peaks F acid G) in the STG. Peaks
A-E were present in the hemolymph of fed, but not starved, lobsters. T
he bioactivity of peaks A-E was tested on the gastric mill rhythm of t
he isolated STG. Only peak E elicited activity. The effects of peak E
included activating the gastric mill rhythm in quiescent preparations
and strengthening existing rhythms in a dose-dependent manner. Further
purification of peak E by high performance liquid chromatography reso
lved this peak into two immunoreactive peaks, one of which retained it
s bioactivity. The effects of peak E were blocked by the CCK antagonis
t proglumide. These results are consistent with a role for peak E in t
he feeding-induced activation of the gastric mill.