Isolation and characterization of two novel peptide amides originating from myelin basic protein in bovine brain.
During a systematic search for peptides that possess the C-terminal amide structure, two novel peptide amides, one with a tyrosine amide and the other with an alanine amide were isolated from bovine brain by acid extraction and sequential steps of reversed phase HPLC. Microsequence, amino acid and mass spectral analyses revealed the structures: Ac-Ala-Ala-Gln-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-Tyr-amide and Ac-Ala-Ala-Gln-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-Tyr-Leu-Ala-Ser-Ala-amide . These 12 and 16 residues peptides had the primary structure identical to the N-terminal fragment of myelin basic protein (MBP). The peptides were therefore designated myelin peptide amide-12 (MPA-12) and -16 (MPA-16). Unlike other amidated peptides, MPA might be generated from MBP by hydroxyl radicals produced via a Fenton reaction in situ. However, this unique amidation seems to occur exclusively to MBP in a site specific manner in the brain.
Takamatsu
K
K
Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, California 94305.
Tatemoto
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry / Q000502:physiology*; D002417:Cattle; D002850:Chromatography, Gel; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry* / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000378:metabolism
D004676:Myelin Basic Protein; D010446:Peptide Fragments; C075345:myelin peptide amide-12; C075346:myelin peptide amide-16