STRUCTURAL-ANALYSIS OF PROTEINS BY CAPILLARY HPLC ELECTROSPRAY TANDEM MASS-SPECTROMETRY

被引：73

作者：

GRIFFIN, PR ^{[1
]}

COFFMAN, JA ^{[1
]}

HOOD, LE ^{[1
]}

YATES, JR ^{[1
]}

机构：

[1] CALTECH,DIV BIOL,139-74,PASADENA,CA 91125

来源：

INTERNATIONAL JOURNAL OF MASS SPECTROMETRY AND ION PROCESSES | 1991年 / 111卷

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0168-1176(91)85052-N

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

Capillary high performance liquid chromatography (HPLC) with on-line ultraviolet detection was coupled with electrospray tandem mass spectrometry. Protein tryptic digests were analyzed at sample levels as low as 800 fmol. Collision-activated dissociation was used to obtain amino acid sequence information on peptides at the 5 pmol level. Protein spotted on to nitrocellulose membrane was digested with trypsin and the resultant peptide mixture was analyzed by capillary HPLC-MS. A deoxynucleotide binding protein isolated by affinity chromatography and sodium dodecylsulfate-polyacrylamide gel electrophoresis was digested in situ and analyzed using this system. The methodology presented in this paper offers a high sensitivity, high throughput strategy for analyzing the primary structure of proteins.

引用

页码：131 / 149

页数：19

共 41 条

[1] INTERNAL AMINO-ACID SEQUENCE-ANALYSIS OF PROTEINS SEPARATED BY ONE-DIMENSIONAL OR TWO-DIMENSIONAL GEL-ELECTROPHORESIS AFTER INSITU PROTEASE DIGESTION ON NITROCELLULOSE [J].