Figure 6.
Figure 6. Biochemical identification of synthetic human SAA1(47-104). (A) Mass spectrometric analysis of synthetic human SAA1(47-104). SAA1(47-104) was chemically synthesized using Fmoc chemistry and was purified via RP-HPLC. The averaged mass spectra, the number of charges for the detected ions, ion intensities, and corresponding mass to charge ratios (m/z) are shown. The insert shows the deconvoluted mass spectrum with the Mr of the uncharged protein calculated using the Bruker deconvolution software. (B) Protein sequences of mature bo SAA1 (UniProt P35541) and hu SAA1α (Uniprot P0DJI8). The bovine SAA1 sequence is aligned with that of human SAA1α and identical amino acids are underlined in the human SAA1α sequence. The insertion of 9 aa in bo SAA1 is indicated with a dashed line. The bo SAA1(46-112) and hu SAA1(47-104) fragments are shaded.

Biochemical identification of synthetic human SAA1(47-104). (A) Mass spectrometric analysis of synthetic human SAA1(47-104). SAA1(47-104) was chemically synthesized using Fmoc chemistry and was purified via RP-HPLC. The averaged mass spectra, the number of charges for the detected ions, ion intensities, and corresponding mass to charge ratios (m/z) are shown. The insert shows the deconvoluted mass spectrum with the Mr of the uncharged protein calculated using the Bruker deconvolution software. (B) Protein sequences of mature bo SAA1 (UniProt P35541) and hu SAA1α (Uniprot P0DJI8). The bovine SAA1 sequence is aligned with that of human SAA1α and identical amino acids are underlined in the human SAA1α sequence. The insertion of 9 aa in bo SAA1 is indicated with a dashed line. The bo SAA1(46-112) and hu SAA1(47-104) fragments are shaded.

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