Isolation and characterization of a novel peptide amide from porcine brain.
Peptide with C-terminal tyrosine amide was isolated from porcine brain by acid extraction and sequential steps of reverse phase HPLC. Microsequence, amino acid and mass spectral analyses revealed the structure: Ac-Ala-Ser-Glu-Lys-Arg-Pro-Ser-Glu-Arg-His-Gly-Ser-Lys- Tyr-amide. Since this peptide had the identical sequence to N-terminus of porcine myelin basic protein (pMBP) 1-14, we have designated porcine myelin peptide amide 14 (pMPA14). The final HPLC step yielded 20 micrograms of homogeneous peptide preparation from 20 kg brain tissue. Unlike other amidated peptides, pMPA14 may be produced by non enzymatic mechanism or unknown amidating enzyme. This unique amidation seems to occur exclusively to MBP in the brain.
Takamatsu
K
K
Department of Psychiatry and Behavioral Sciences Stanford University School of Medicine CA 94305.
Tatemoto
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002851:Chromatography, High Pressure Liquid; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000302:isolation & purification*; D013552:Swine
D004676:Myelin Basic Protein; D010446:Peptide Fragments; C066466:myelin basic protein 1-14