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Journal Article

A peptide with N-terminal histidine and C-terminal isoleucine amide (PHI) and vasoactive intestinal peptide (VIP) are copackaged in myenteric neurones of the guinea pig ileum.

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Agoston,  D.
Abteilung Neurochemie, MPI for biophysical chemistry, Max Planck Society;

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Whittaker,  V. P.
Abteilung Neurochemie, MPI for biophysical chemistry, Max Planck Society;

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Citation

Agoston, D., Fahrenkrug, J., Mikkelsen, J. D., & Whittaker, V. P. (1989). A peptide with N-terminal histidine and C-terminal isoleucine amide (PHI) and vasoactive intestinal peptide (VIP) are copackaged in myenteric neurones of the guinea pig ileum. Peptides, 10(3), 571-573. doi:10.1016/0196-9781(89)90144-7.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-49B6-4
Abstract
When cytoplasmic extracts of the myenteric plexus of guinea pig ileum are submitted to centrifugal density gradient separation in a zonal rotor, conditions which separate storage particles containing substance P, somatostatin and VIP from each other, PHI copurifies with VIP. The two immunoreactivities cannot be separated by particle exclusion chromatography, which depends on size rather than density. It is concluded that the posttranslational cleavage of the propeptide or precursor to PHI and VIP occurs after packaging into these storage particles.