Tandem Mass Spectrometry Analysis of Fibrils from Tissue Deposits in a Patient with Primary Amyloid Disease

摘要

Although we have successfully used multiple analytical methods to characterize immunoglobulin light chain (Ig LC) proteins from the urine and blood of patients with primary amyloidosis (AL), the highly insoluble fibrillar deposits themselves are more refractory to structural analysis. The studies reported here are focused on the fibrils purified from patient organs and imaged by Atomic Force Microscopy (AFM). The recent installation of an LTQ-Orbitrap hybrid mass spectrometer system has now enabled us to acquire more complete information for protein identification and determination of post-translational modifications, thus extending the results obtained during preliminary analyses that utilized MALDI-TOF MS and MALDI Q-o-TOF MS.