This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. MALDI-TOF-MS was performed with a Voyager mass spectrometer operated in the positive ion mode. For the peptide samples, the mass spectrometer was calibrated with a mixture of proteins. Aqueous solutions of samples were diluted 1:1 with alpha-cyano-4-hydroxycinnamic acid and a portion (1.0 l) was applied to the sample plate of the MS. Samples were desorbed from the sample plate with a nitrogen laser having an accelerating voltage intensity of 20000V and a laser intensity of approximately 1300. For the carbohydrates sample, the mass spectrometer was calibrated with a mixture of dextrans. An aqueous solution of the sample was diluted 1:1 with 2,5-dihydroxybenzoic acid and a portion (1.0 l) was applied to the sample plate of the MS. Samples were desorbed from the sample plate with a nitrogen laser having an accelerating voltage intensity of 20000V and a laser intensity of approximately 1800.
Showing the most recent 10 out of 104 publications