Application of multidimensional affinity high-performance liquid chromatography and electrospray ionization liquid chromatography mass spectrometry to the characterization of glycosylation in single-chain plasminogen activator Initial results

被引：12

作者：

Apffel, A ^{[1
]}

Chakel, JA ^{[1
]}

Hancock, WS ^{[1
]}

Souders, C ^{[1
]}

MTimkulu, T ^{[1
]}

Pungor, E ^{[1
]}

机构：

[1] BERLEX BIOSCI,BRISBANE,CA 94005

来源：

JOURNAL OF CHROMATOGRAPHY A | 1996年 / 750卷 / 1-2期

关键词：

glycosylation; plasminogen activator; glycoproteins; proteins;

D O I：

10.1016/0021-9673(96)00528-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Preliminary results are presented using a combination of affinity chromatography, reversed-phase HPLC and electrospray ionization mass spectrometry to produced peptide maps for N-linked, O-linked and non-glycosylated peptides from an endoproteinase LysC digest of DSPA alpha 1, a recombinant DNA derived glycoprotein. Although the system was used to identify a number of major N-linked structures, notably complex biantennary structures attached to asparagine 362, no O-linked glycopeptides from the possible 4 attachment sites were identified. The system did, however, demonstrate the feasibility of the approach and the applicability of the instrumental system.

引用

页码：35 / 42

页数：8

共 9 条

[1] ENHANCED SENSITIVITY FOR PEPTIDE-MAPPING WITH ELECTROSPRAY LIQUID-CHROMATOGRAPHY MASS-SPECTROMETRY IN THE PRESENCE OF SIGNAL SUPPRESSION DUE TO TRIFLUOROACETIC ACID-CONTAINING MOBILE PHASES [J].