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. 2014 Oct 27;9(10):e111363. doi: 10.1371/journal.pone.0111363

Table 2. Serpin cleavage sites determined by MALDI-TOF-MS.

Serpin m/z determined Theoretical mass Deviation (ppm) Sequence Position
α1-PI 4133.333 4133.234 +24 380IPM-SIP385 Reactive bond
α1-AC 4623.419 4623.495 −16 381TLL-SAL386 Reactive bond
AGT 4299.351 4299.293 +14 444QQL-NKP449 Reactive center loop
α2-AP 2181.123 2181.097 +12 45SPL-TLL50 N-terminal extension
α2-AP 3489.789 3489.788 <1 458QSL-KGF463 C-terminal extension
α2-AP 3602.870 3602.872 −1 457LQS-LKG462 C-terminal extension
α2-AP 5308.3 (average) 5307.9 (average) +75 442REL-KEQ447 C-terminal extension

Given are masses determined by MALDI-TOF-MS directly after incubation of serpin with EspPα, theoretical masses, mass deviation, according sequence, and position inside the serpin sequence. Numeration is according to the serpin precursor.