MALDI-ISD Measurements Using Both the SpiralTOF Mode and the LinearTOF Mode March 5, 2020 Application Note, MALDI SpiralTOF™, Mass Spectrometry (MS) 0 Introduction Matrix assisted laser desorption/ionization (MALDI) combined with in-source decay (ISD) is a useful tool for doing top-down sequencing of intact proteins. In this work, we measured and compared the ISD fragment ions generated for several proteins by using both the high resolution MALDI-Spiral mode and the high sensitivity MALDI-Linear mode available on the JEOL SpiralTOF MALDI-MS system. Experimental Myoglobin and Bovine serum albumin (BSA) protein samples were separately dissolved into 0.1% trifluoroacetic acid aqueous with the concentration fixed at 10 pmol/μL. 1,5-diaminonaphthalene (DAN), which can provide good S/N for ISD fragment ions [1], was used as the MALDI matrix. The DAN matrix was dissolved to 0.1% trifluoroacetic acid aqueous/ 50% acetonitrile with the matrix concentration fixed at 10 mg/mL. Subsequently, the matrix and the sample solutions were mixed 1/1 (v/v), and then 1 μL of each solution was deposited and dried on the MALDI target plate. Afterwards, each sample was analyzed in triplicate on the JEOL JMS-3000 SpiralTOF by using both the SpiralTOF mode and the LinearTOF mode. For full details: Attached files often contain the full content of the item you are viewing. Be sure and view any attachments. MALDI-ISD Measurements Spiral and Linear.pdf 1.27 MB Showing 0 Comment Comments are closed.