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. 2018 Jun 4;9:1081. doi: 10.3389/fimmu.2018.01081

Table 1.

Mass spectrometric analysis of the cleavage sites of matrix metalloproteinase-9 (MMP-9) in intact recombinant SAA1α.

a.a. Intact serum amyloid A1 (SAA1) protein sequence
1–104b RSFFSFLGEAFDGARDMWRAYSDMREANYIGS DKYFHARGNYDAAKRGPGG
VWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY

COOH-terminal SAA1 peptide sequence Rel. int. (%),a 3 h

52–104 VWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY 29.9
57–104       AISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY 19.8
58–104      ISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY 50.3

aRelative intensity (%) of the SAA1(52–104), SAA1(57–104), and SAA1(58–104) peptides after incubation for 3 h of intact SAA1α (Uniprot P0DJI8) with MMP-9 (E:S ratio 1:50) and subsequent analysis by mass spectrometry.

bThe amino acid (a.a.) sequence of SAA1(1–51) is underlined in the intact protein sequence.