Takamatsu K, Tatemoto K
Department of Psychiatry and Behavioral Sciences Stanford University School of Medicine CA 94305.
Biochem Biophys Res Commun. 1990 Nov 15;172(3):1167-74. doi: 10.1016/0006-291x(90)91571-9.
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.
通过酸提取和反相高效液相色谱的连续步骤，从猪脑中分离出了C末端为酪氨酸酰胺的肽。微序列分析、氨基酸分析和质谱分析揭示了其结构：Ac-Ala-Ser-Glu-Lys-Arg-Pro-Ser-Glu-Arg-His-Gly-Ser-Lys-Tyr-酰胺。由于该肽与猪髓鞘碱性蛋白（pMBP）1-14的N末端序列相同，我们将其命名为猪髓鞘肽酰胺14（pMPA14）。最终的高效液相色谱步骤从20千克脑组织中获得了20微克的纯肽制剂。与其他酰胺化肽不同，pMPA14可能是通过非酶机制或未知的酰胺化酶产生的。这种独特的酰胺化似乎仅在脑中的髓鞘碱性蛋白中发生。
