Gibson B W, Gilliom R D, Whitaker J N, Biemann K
J Biol Chem. 1984 Apr 25;259(8):5028-31.
In order to resolve the uncertainties about the primary structure of human myelin basic protein at residues 45-89, the sequence of this peptide and its tryptic fragments were reinvestigated by fast atom bombardment mass spectrometry. The sequence at positions 77-78 was found to be His-Gly and the sequence at positions 83-84 was shown to be Glu-Asn. The Ser at position 56 was not phosphorylated, whereas the residue at position 46 or 47 showed a heterogeneity of Gly and Ser in this peptide fragment in one of two protein preparations from different patients. These results demonstrate the usefulness of fast atom bombardment mass spectrometry for primary structure information. The corrected sequence of human basic protein peptide 45-89 will permit a more detailed immunochemical analysis of this peptide and its in vivo degradation products.
为了解决人髓鞘碱性蛋白45 - 89位残基一级结构的不确定性，通过快原子轰击质谱法对该肽段及其胰蛋白酶消化片段的序列进行了重新研究。发现77 - 78位的序列为His - Gly，83 - 84位的序列为Glu - Asn。56位的丝氨酸未被磷酸化，而在来自不同患者的两种蛋白质制剂之一的该肽片段中，46或47位的残基显示出甘氨酸和丝氨酸的异质性。这些结果证明了快原子轰击质谱法在获取一级结构信息方面的有用性。人碱性蛋白肽45 - 89的校正序列将有助于对该肽段及其体内降解产物进行更详细的免疫化学分析。
