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Plasma desorption mass spectrometry coupled with conventional peptide sequencing techniques
A G Craig1, A Engström, H Bennich
1Department of Immunology, University of Uppsala, Sweden.
Biomedical & Environmental Mass Spectrometry
|November 1, 1987
Summary
Researchers determined the mass of the antibacterial protein cecropin B using 252Cf plasma desorption time-of-flight mass spectrometry. This analysis established the protein's carboxy terminal amino acid sequence.
Area of Science:
- Biochemistry
- Proteomics
- Insect Biochemistry
Background:
- Cecropin B is an antibacterial protein found in the Chinese oak silk moth (Antherea pernyi).
- Understanding protein structure is crucial for elucidating biological function.
- Mass spectrometry offers precise molecular weight determination.
Purpose of the Study:
- To determine the precise mass of intact cecropin B.
- To analyze enzymatically derived fragments of cecropin B.
- To establish the carboxy terminal amino acid sequence of cecropin B.
Main Methods:
- 252Cf plasma desorption time-of-flight mass spectrometry was employed.
- Intact cecropin B was analyzed.
- Enzymatically generated fragments of cecropin B were analyzed.
Main Results:
- The mass of intact cecropin B was accurately measured.
- Masses of enzymatically derived fragments were determined.
- The carboxy terminal amino acid sequence was established based on mass data.
Conclusions:
- 252Cf plasma desorption time-of-flight mass spectrometry is effective for protein mass determination.
- The study successfully elucidated the carboxy terminal sequence of cecropin B.
- This structural information contributes to the understanding of cecropin B's antibacterial activity.