LC-MS and MALDI MS Investigation of Tryptic Protein Digestion: Towards Protein Digestion Standards

Library Number:
WA40497
Part Number:
WA40497
Author(s):
Amy E Daly;Martin Gilar;Ying-Qing Yu;Bonnie A Alden;John C Gebler;[Waters]
Source:
ASMS, HPLC
Content Type:
Posters
Content Subtype:
ASMS
Compounds:
Enolase tryptic digest; ADH tryptic digest; BSA tryptic digest; Phosphorylase tryptic digest;; Hemoglobin tryptic digest
Related Products:
 
Proteolysis is thought to be a well understood process, however, many exceptions to the basic cleavage rule (cleave after K or R, but not when followed by P) have been reported. The protein digests are typically more complex than predicted or desired. In this study the selected proteins were digested and analyzed by LC-MS, LC-MS/MS, and MALDI MS in order to evaluate the fidelity of trypsin. The examples demonstrating the variability of proteolytic cleavage are given. This variability makes it difficult to use protein digests as HPLC and MS standards and potentially complicates the proteome analysis of global protein digests. Methods:

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