COMBINED PLASMA-DESORPTION MASS-SPECTROMETRY AND EDMAN DEGRADATION APPLIED TO SIMULTANEOUS SEQUENCE DETERMINATION OF ISOFORMS OF STRUCTURAL PROTEINS FROM THE CUTICLE OF LOCUSTA-MIGRATORIA

被引:13
作者
ANDREASEN, L
HOJRUP, P
ANDERSEN, SO
ROEPSTORFF, P
机构
[1] ODENSE UNIV,DEPT MOLEC BIOL,DK-5230 ODENSE,DENMARK
[2] UNIV COPENHAGEN,AUGUST KROGH INST,DK-2100 COPENHAGEN,DENMARK
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 217卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1993.tb18242.x
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
The primary structures of two basic low-molecular-mass proteins, Lm-67 and Lm-70 from the pharate cuticle of the migratory locust, Locusta migratoria, were determined. The sequencing strategy was based on combined use of plasma-desorption mass spectrometry (PDMS) and automatic Edman degradation of the proteins and their enzymically derived peptides. The mass-spectral data showed the presence of two proteins in each preparation. For protein preparation Lm-67, this was indicated by the mass spectrum of the intact protein. For protein preparation Lm-70, the presence of two variants only became evident by mass-spectrometric analysis of the enzymically derived peptides. Both proteins show strong similarity to other exocuticular proteins from L. migratoria.
引用
收藏
页码:267 / 273
页数:7
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