## Abstract For interrogation of peptides with diverse modifications, no other instrument is as versatile as the Fourier‐transform mass spectrometer (FTMS). Particularly using electrospray ionization (ESI), many intact proteins and their proteolytic products harboring post‐translational and chemica
High-resolution tandem mass spectra of 37-67 kDa proteins
✍ Scribed by J. Paul Speir; Michael W. Senko; Daniel P. Little; Joseph. A. Loo; Fred W. McLafferty
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 394 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1076-5174
No coin nor oath required. For personal study only.
✦ Synopsis
By dissociating noncovalent adducts with infrared radiation and minimizing ion charge density during measurement, Fourier-transform mass spectrometry with electrospray ionization yields 160 000 resolving power for porcine albumin. Its molecular weight calculated from the published sequence is 66 740, but values found for two different samples are MW = 66736 and 66886. The spectrum of their mixture confirms this mass difference. Similar measurements of two Protein A (45 kDa) samples also give molecular weights in substantial disagreement with literature sequences. Tandem mass spectrometry gives partial sequence information that demonstrates errors in some of the reported sequences.
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A technique for the recording of complete high resolution mass spectra (resolving power : 1 part in 10 000 or better) of compounds emerging from a gas chromatograph is discussed. The pressure reduction system used for the connection of chromatographic column and mass spectrometer is short, simple in