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. Author manuscript; available in PMC: 2022 May 1.
Published in final edited form as: J Leukoc Biol. 2020 Oct 18;109(5):915–930. doi: 10.1002/JLB.3A0720-422R

Fig. 2: Purification and characterization of nAGP-1 in comparison with sAGP-1:

Fig. 2:

Elution profile of (A) PAF-induced Neutrophil supernatant (nAGP-1) and (B) serum derived AGP-1 (sAGP-1) on DEAE-Cellulose column. The insets represent the elution profile of nAGP-1 (A inset) and sAGP-1 (B inset) on Cibacron blue column respectively. The fraction(s) containing the respective AGP-1 is indicated by red arrow. (C) and (D) Western blotting analysis of different fractions of DEAE-cellulose column against nAGP-1 and sAGP-1 respectively (two different gels) indicated by red arrow. (E) Mass spectral analysis of commercial AGP-1, sAGP-1 and nAGP-1. The data revealed that the protein components of the two AGP-1s are identical. Glycomic analysis of (F) commercial AGP-1 and (G) sAGP-1 showed that these two preparations are similar. (H) nAGP-1 differed in glycosylation complexity and composition when compared to sAGP1. graphic file with name nihms-1636436-ig0010.jpg - N-Acetyl Glucoseamine; graphic file with name nihms-1636436-ig0011.jpg- Mannose; graphic file with name nihms-1636436-ig0012.jpg- Galactose; graphic file with name nihms-1636436-ig0013.jpg - Fucose; graphic file with name nihms-1636436-ig0014.jpg - Sialic acid. (I) % relative abundance of sialylated, non-sialylated, high-mannose, mono- di- and tri+ - sialylated N-glycans present in commercial AGP-1, sAGP-1 and nAGP-1.