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Identification and characterization of variant forms of the gastrin‐releasing peptide (GRP)
Author(s) -
McDonald T.J.,
Jörnvall H.,
Tatemoto K.,
Mutt V.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80527-4
Subject(s) - gastrin releasing peptide , identification (biology) , peptide , characterization (materials science) , gastrin , chemistry , biochemistry , biology , bombesin , neuropeptide , secretion , materials science , nanotechnology , receptor , botany
Porcine intestinal gastrin‐releasing peptide (GRP) has been demonstrated to be structurally identical to the previously characterized gastric GRP. Ion‐exchange and high‐performance liquid chromatography of porcine intestinal extracts have identified two variant GRP forms. Studies on one of these variant forms suggest that a β‐aspartyl shift has occurred in the Asn—His structure of GRP; such a modification in an Asn—His structure occurring in a natural peptide or protein has not been previously reported. This variant GRP, although retaining bioactivity, appears to have reduced potency in elevating canine plasma gastrin levels.

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