RAPID METHOD BASED ON REVERSED-PHASE HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY FOR PURIFICATION OF HUMAN MYELIN BASIC-PROTEIN AND ITS THROMBIC AND ENDOPROTEINASE LYS-C PEPTIDES

被引：7

作者：

GIEGERICH, G ^{[1
]}

PETTE, M ^{[1
]}

FUJITA, K ^{[1
]}

WEKERLE, H ^{[1
]}

EPPLEN, JT ^{[1
]}

HINKKANEN, A ^{[1
]}

机构：

[1] MAX PLANCK GESELL,FORSCH GRP KLIN,W-8700 WURZBURG,GERMANY

来源：

JOURNAL OF CHROMATOGRAPHY-BIOMEDICAL APPLICATIONS | 1990年 / 528卷 / 01期

关键词：

D O I：

10.1016/S0378-4347(00)82364-6

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Reversed-phase high-performance liquid chromatography was applied to isolate myelin basic protein from human brain, followed by separation of proteolytic peptides thereof on the same chromatographic system. Brain tissue was delipidated under conditions that keep copurifying protease inactive. The crude brain protein fraction was applied directly to a C4 column. The homogeneous protein obtained in this way was digested with thrombin and endoproteinase Lys-C in order to produce short defined myelin basic protein peptides. The purified peptides were used to determine the antigen fine specificity of myelin basic protein recognizing T lymphocyte lines isolated from multiple sclerosis patients. © 1990.

引用

页码：79 / 90

页数：12

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