Chemical detection of natural peptides by specific structures. Isolation of chicken galanin by monitoring for its N-terminal dipeptide, and determination of the amino acid sequence.
We have isolated galanin from chicken intestine by monitoring for the N-terminal glycyltryptophan, which constitutes a conserved part characteristic of the peptide. This monitoring method complements that previously used for C-terminal amide detection and proves chemical monitoring of specific structures to be useful. The isolation allowed determination of the structure, which was found to be unidentical to any of the known galanins. However, N-terminal pentadecapeptide parts are identical, showing this segment to be of special importance. In addition to common substitutions at positions 16, 18, 23, 26 and 29, chicken galanin has phenylalanine at position 28, where all known mammalian galanins have leucine.
Norberg
A
A
Department of Biochemistry II, Karolinska Institute, Stockholm, Sweden.
Sillard
R
R
Carlquist
M
M
Jörnvall
H
H
Mutt
V
V
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002845:Chromatography; D004151:Dipeptides / Q000302:isolation & purification*; D019004:Galanin; D007422:Intestines / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid
D004151:Dipeptides; D010446:Peptide Fragments; D010455:Peptides; C032120:glycyltryptophan; D019004:Galanin