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UV‐laser‐induced desorption mass spectrometry of insulin, substance P and A4 amyloid protein fragments from synthetic fibrillary aggregates
Author(s) -
Perera I. K.,
Candy J. M.,
Håkansson P.,
Oakley A. E.,
Brinkmalm G.,
Sundqvist B. U. R.
Publication year - 1990
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290041212
Subject(s) - chemistry , mass spectrometry , molecular mass , glial fibrillary acidic protein , fibril , desorption , amyloid (mycology) , chromatography , biochemistry , biophysics , organic chemistry , enzyme , medicine , inorganic chemistry , immunohistochemistry , adsorption , biology
Matrix‐assisted UV‐laser‐induced desorption has previously enabled the molecular weights of non‐aggregated peptides, polypeptides and proteins to be determined using mass spectrometry. We now report that this technique can be used to disaggregate and determine the molecular weights of peptides, polypeptides and proteins, present as β‐pleated sheet fibrillary polymers. It was found that the molecular weights of the individual fibril constituents could be determined at subpicomolar concentrations and at a high accuracy. The unrivalled sensitivity and ability to disaggregate fibrillary proteins show the potential of this technique for characterizing the proteins associated with pathological features which occur in a number of diverse disease states.