2-DIMENSIONAL ELECTROPHORESIS AS A COMPLEMENTARY METHOD OF ISOLATING PEPTIDE-FRAGMENTS OF CLEAVED PROTEINS FOR INTERNAL SEQUENCING

被引：2
|
作者：
NOKIHARA, K [1 ]
KURIKI, T [1 ]
MORITA, N [1 ]
机构：
[1] TOKYO UNIV AGR & TECHNOL,KOGANEI,TOKYO,JAPAN
来源：
JOURNAL OF CHROMATOGRAPHY A | 1994年 / 676卷 / 01期
关键词：
D O I：
10.1016/0021-9673(94)00091-3
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
To determine the primary structure of proteins, usually proteolytic enzyme digests are separated by reversed-phase high-performance liquid chromatography (HPLC) and each fraction is collected and sequenced. The results obtained by different cleavages are combined to reveal the entire sequence. However, there are many N-terminal-blocked proteins and/or intact proteins or their particular fragments that are not eluted from HPLC columns. Internal fragments of such proteins were successfully isolated by the use of two-dimensional electrophoresis, after digestion. Electroblotted spots were easily sequenced to identify those difficult fragments which could not be obtained using HPLC.
引用
收藏
页码：233 / 238
页数：6
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