SEQUENCE-ANALYSIS OF PHOSPHOSERINE-CONTAINING PEPTIDES - MODIFICATION FOR PICOMOLAR SENSITIVITY
SEQUENCE-ANALYSIS OF PHOSPHOSERINE-CONTAINING PEPTIDES - MODIFICATION FOR PICOMOLAR SENSITIVITY
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DOI：
10.1016/0014-5793(86)81388-6
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发表时间：
1986-08-11
期刊：
影响因子：
3.5
通讯作者：
HEILMEYER, LMG
中科院分区：
文献类型：
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作者：
MEYER, HE;HOFFMANNPOSORSKE, E;HEILMEYER, LMG
对含有磷酸丝氨酸的多肽进行测序，通常在磷酸丝氨酸所在的位置上没有可识别的PTH-衍生物。这里描述了一种新的方法，它允许在序列分析之前通过化学修饰来鉴定磷酸丝氨酸的位置。在一步微批反应中，完整多肽中的磷酸丝氨酸可以定量地转化为稳定的衍生物，如β-甲氨基丙氨酸、S-乙醇半胱氨酸或乙基半胱氨酸。在使用配有在线PTH氨基酸分析仪的应用生物系统气相测序仪进行微测序时，可以检测到这些衍生物，其多肽含量低于100 pmoL。
Sequencing of phosphoserine‐containing peptides yields normally no identifiable PTH‐derivatives at those positions where phosphoserine is located. Here a new method is described which allows identification of the position of phosphoserine by chemical modification just before sequence analysis. In a one‐step microbatch reaction, phosphoserine present in the intact peptide can be transformed quantitatively into stable derivatives such as β‐methylaminoalanine (MAA),S‐ethanolcysteine orS‐ethylcysteine. These derivatives are detectable during microsequencing with less than 100 pmol peptide using an Applied Biosystems gas‐phase sequencer equipped with an on‐line PTH amino acid analyzer.