Skip to main content
. 2008 Feb 22;105(9):3232–3237. doi: 10.1073/pnas.0710412105

Fig. 2.

Fig. 2.

Analysis of MUC1a peptide expressed in engineered yeast cells. (a) MALDI-TOF MS spectra of each exogenously expressed MUC1a peptide. MUC1a produced by N-1, TN-1, and T-1 cells show MUC1a/N-1, MUC1a/TN-1, and MUC1a/T-1, respectively. The molecular mass of MUC1a is 1,932. (b) Lectin microarray. BPL, Bauhinia purpurea lectin; ABA, Agaricus bisporus agglutinin; Jacalin, Artocarpus integrifolia lectin; PNA, peanut agglutinin; WFA, Wisteria floribunda agglutinin; ACA, Amaranthus caudatus agglutinin; MPA, Maclura pomifera agglutinin; HPA, Helix pomatia agglutinin; VVA, Vicia villosa agglutinin. GalNAc binders: Jacalin, WFA, MPA, HPA, and VVA; core1 binders: ABA, PNA, and ACA; core1 and GalNAc binder: BPL. (c) Enzymatic digestion of MUC1a/T-1. The peak at 24.5 min corresponds to a core1-MUC1a peptide, whereas the peak at 25.1 min corresponds to the GalNAc-MUC1a peptide. (d) Inhibition of yeast O-mannosylation with a chemical reagent. MUC1a was expressed in TN-1 strains in the presence or absence of R3A-1c reagent. The total area of the recombinant MUCla peak on the chromatogram is set to 100%, and error bars show standard deviation of the mean (n = 3).