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. Author manuscript; available in PMC: 2026 Sep 1.
Published in final edited form as: Carbohydr Res. 2026 Jun 26;567:110019. doi: 10.1016/j.carres.2026.110019

Fig. 2.

Fig. 2.

Comparison of E. coli expressed human and bovine B4GalT1 in producing G2-trastuzumab glycoform. A) Time course profile of the hB4GalT1-and bB4GalT1-catalyzed Gal transfer from UDP-Gal to trastuzumab (n = 1). B) Charge deconvoluted LC-MS of the Fc domain of native trastuzumab after IdeS treatment (G0: expected 25,229.7 Da, found 25,231.0 Da; G1, expected 25,391.7 Da, found 25,392.0 Da; G2, expected 25,553.8 Da, found 25,555.0 Da). C) Charge deconvoluted LC-MS of the Fc domain of G2-trastuzumab (1) after IdeS treatment (expected, 25,553.8 Da; found, 25,555.0 Da) Enzymatic reaction conditions: A mixture of trastuzumab (25 mg/ml), UDP-Gal (15 eq), and hB4GalT1 or bB4GalT1 (5%, w/w, enzyme: antibody) was incubated in a buffer containing 10 mM MnCl 2 (pH 7.4) at 37 °C. The reactions were monitored by LC-MS analysis of the Fc fragment released by IdeS treatment of the antibodies.