Literature DB >> 8223564

Combined plasma-desorption mass spectrometry and Edman degradation applied to simultaneous sequence determination of isoforms of structural proteins from the cuticle of Locusta migratoria.

L Andreasen1, P Højrup, S O Andersen, P Roepstorff.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1993        PMID: 8223564     DOI: 10.1111/j.1432-1033.1993.tb18242.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  1 in total

1.  Isoforms of a cuticular protein from larvae of the meal beetle, Tenebrio molitor, studied by mass spectrometry in combination with Edman degradation and two-dimensional polyacrylamide gel electrophoresis.

Authors:  S Haebel; C Jensen; S O Andersen; P Roepstorff
Journal:  Protein Sci       Date:  1995-03       Impact factor: 6.725

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.