Abstract:
:A new method for complementing existing protein chemical techniques for the assignment of S-S bridge positions in amino-acid sequences is described. The principle of the method is the direct examination of the masses of protein fragments, obtained by chemical or enzymatic degradation. Proteins are digested under conditions known to minimise disulphide reduction and reshuffling, and the unfractionated digest is examined directly by high field magnet (or other high mass) fast atom bombardment or Californium mass spectrometry. Disulphide linked peptides are identified from their unique masses, and by comparison with the spectrum of digested and reduced samples in which the signal corresponding to the S-S linked peptide(s) is replaced by two signals corresponding to the respective thiol peptide components, if INTER-bridged, or shifted by two mass units (dithiol) if INTRA-bridged. This rapid procedure has considerable potential in assisting with studies on the primary structure of proteins, in crystallographic studies and the monitoring of denaturation/renaturation of recombinant proteins.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Morris HR,Pucci Pdoi
10.1016/0006-291x(85)90302-xsubject
Has Abstractpub_date
1985-02-15 00:00:00pages
1122-8issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(85)90302-Xjournal_volume
126pub_type
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