Variant forms of galanin isolated from porcine brain.
In a peptide concentrate, prepared from acid extracts of porcine brain, several galanin-like immunoreactive peptides were detected and two of these were purified. Characterization of the peptides by sequence analysis, mass spectrometry, and capillary zone electrophoresis identified them as a N-terminally nine residue elongated form of galanin, preprogalanin(24-61) amide, and as an N-terminally four residue truncated form of galanin corresponding to preprogalanin(37-61) amide. The former finding suggests that the removal of the signal peptide in preprogalanin occurs by enzymatic cleavage between glycine-23 and leucine-24. The presence of truncated galanin might refer to a mechanism, where galanin is inactivated by removal of functionally important amino acid residues from the N-terminus.
Sillard
R
R
Department of Biochemistry II, Karolinska Institutet, Stockholm, Sweden.
Rökaeus
A
A
Xu
Y
Y
Carlquist
M
M
Bergman
T
T
Jörnvall
H
H
Mutt
V
V
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry / Q000502:physiology*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D019004:Galanin; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000302:isolation & purification*; D010455:Peptides / Q000302:isolation & purification*; D011863:Radioimmunoassay; D017386:Sequence Homology, Amino Acid; D013552:Swine
D009479:Neuropeptides; D010455:Peptides; D019004:Galanin