FAST-ATOM-BOMBARDMENT MASS-SPECTROMETRY AND CHEMICAL-ANALYSIS IN DETERMINATIONS OF ACYL-BLOCKED PROTEIN STRUCTURES

被引:15
作者
EGESTAD, B
ESTONIUS, M
DANIELSSON, O
PERSSON, B
CEDERLUND, E
KAISER, R
HOLMQUIST, B
VALLEE, B
PARES, X
JEFFEREY, J
JORNVALL, H
机构
[1] KAROLINSKA INST,DEPT PHYSIOL CHEM,S-10401 STOCKHOLM 60,SWEDEN
[2] UNIV ABERDEEN MARISCHAL COLL,DEPT MOLEC & CELL BIOL,ABERDEEN AB9 1AS,SCOTLAND
[3] HARVARD UNIV,CTR BIOCHEM & BIOPHYS SCI & MED,BOSTON,MA 02115
[4] UNIV AUTONOMA BARCELONA,DEPT BIOQUIM & BIOL MOLEC,BARCELONA,SPAIN
关键词
Blocked peptide; C-terminal determination; Fast atom bombardment; Mass spectrometry; N-terminal acetylation;
D O I
10.1016/0014-5793(90)81152-E
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Peptide generation and fast atom bombardment mass spectrometry in combination with conventional chemical analysis was used to identify the blocking group and establish the N-terminal structure of six different proteins at the nanomole level. In this manner, the first terminal structures of three non-mammalian alcohol dehydrogenases were determined, demonstrating the presence of N-terminal acetylation in these piscine, amphibian, and avian enzymes. Similarly, two different yeast glucose-6-phosphate dehydrogenases and a minor variant of a human alcohol dehydrogenase were found to be acetylated. The exact end location of C-terminal structures was also established. Together, the analyses permit the definition of terminal regions and blocking groups, thus facilitating the delineation of remaining structures. © 1990.
引用
收藏
页码:194 / 196
页数:3
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