J. Biol. Chem., Vol. 262, Issue 33, 15886-15889, Nov, 1987
Isolation, structures, and biologic activity of neurotensin-related peptides generated in extracts of avian tissue
RE Carraway, DE Cochrane and SE Ruane
Department of Physiology, University of Massachusetts Medical Center, Worcester 01605.
Two immunoreactive neurotensin-related peptides generated by the action of
endogenous protease(s) on protein substrates during acid extraction of
avian tissues have been isolated from extracts of turkey skin and
proventriculus. One was identified as the pentadecapeptide, H-Phe-Glu-
Arg-Phe-Gln-Gly-Met-Arg-Thy-Arg-Gly-Pro-Tyr-Phe-Leu-OH and the other was
its C-terminal octapeptide fragment. Each peptide showed partial homology
to the C-terminal, biologically active region of avian neurotensin, and
isolated preparations displayed pharmacologic activity at submicromolar
concentrations. Synthetic preparations were shown to be indistinguishable
from the native peptides during high pressure liquid chromatography (HPLC)
and bioassay. Analysis by HPLC indicated that similar peptides could be
generated in extracts of proventriculus, pancreas, small intestine, skin,
heart, lung, and skeletal muscle. These results, establishing the presence
of a neurotensin-related sequence which can be liberated from protein(s) by
the action of tissue enzyme(s), suggest that peptide(s) similar to
neurotensin may be rapidly formed in order to promote physiologic
regulation in multiple tissue(s).
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