X-Ray Absorption and Emission In Analytical Chemistry by H. A. Liebhafsky, H. G. Pfeiffer, E. H. Winslow, P. D.

By H. A. Liebhafsky, H. G. Pfeiffer, E. H. Winslow, P. D. Zemany

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Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Science 1989;246:6471. Karas M, Hillenkamp F. Anal Chem 1988;60:2299-2301. Carr SA, Hemling ME, Bean MF, Roberts GD. Anal Chem 1991;63:2802-2824. Chait BT, Kent SB. Science 1992;257: 1885-1894. Aebersold R, Hess D, Morrison HD, Yungwirth T, Chow DT, Affolter M, Amankwa LN. J Protein Chem 1994;13:465-466. Hopfgartner G, Wachs T, Bean K, Henion J. Anal Chem 1993;65:439-446. Tomer KB, Moseley MA, Deterding LJ. Parker CE. Mass Spectrom Rev 1994;13: 431 -457.

Isomerization of the N-terminal peptide fragment obtained after tryptic digestion of rSmp2812 can be explained by the fact that the peptide contains a cyclic linkage that formed during digestion. Since this phenomenon was only observed in the case of rSmp2812, it is likely to be related to the original N-terminal modification that led to the shift in isoelectric point. To test the hypothesis of a cyclic linkage, both the free and blocked Nterminal peptides were subjected to deuterium exchange followed by MS.

9). After detergent removal by acetone precipitation, intact rOspA was submitted to an acidic methanol treatment in order to generate fatty acid methyl esters via transmethylation. Fatty acid methyl esters were extracted into hexane, which permitted their analy- Bischoff and Bouchon S-[2,3-Bis(palmitoyloxy)-(2RS)-propyl]-N-palmitoyl-(R)-cysteinyl ("Pam3Cys")configuration (A2, A3, A4, ... : amino acids) Figure 9 Structure of the lipidated N-terminal tryptic peptide CK of rOspA containing three palmitoyl residues.

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