Observation of noncovalent complexes to the avidin tetramer by electrospray ionization mass spectrometry
β Scribed by Brenda L. Schwartz; Karen J. Light-Wahl; Richard D. Smith
- Book ID
- 103995848
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 370 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1044-0305
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β¦ Synopsis
Intact avidin-biotin and avidin-biotin maleimide noncovalent complexes have been observed by electrospray ionization mass spectrometry (ESI-MS) by using an extended mass range quadrupole mass spectrometer. By utilizing mild ES1 interface conditions, the expected solution behavior of four biotin or biotin maleimide molecules noncovalently binding to each avidin tetramer can be preserved in the gas phase. The ESI-MS results show the appropriate mass additions of 973 Β± 60 Da for biotin and 1802 Β± 40 Da for biotin maleimide to the avidin tetramer species. These results support the hypothesis that substantial retention of higher order structure is possible in the gas phase by using gentle ESI conditions.
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## Abstract Mass spectrometry with electrospray ionization and a magnetic sector instrument was used to detect multiply charged molecules for the nonβcovalently bound dimeric subunit protein complexes of horse liver alcohol dehydrogenase (__M__~r~ βΌ 80 000) and the tetrameric complexes of yeast alc