Skip to main content
. 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. 3.

Fig. 3.

Comparative analysis of the E. coli expressed human and bovine B4GalT1 mutants for transferring GalNAc to G0 antibody glycoform. A) time course profile of the hB4GalT1-Y285L and bB4GalT1-Y289L catalyzed transfer of GalNAc to G0 antibody glycoform (2) to yield the LacdiNAc trastuzumab (3) (n = 2). B) Charge deconvoluted LC-MS of the Fc domain of the GalNAc2-trastuzumab (3) after IdeS treatment (expected, 25,635.7 Da, found 25637.0 Da) Enzymatic reaction conditions: A mixture of the G0-trastuzumab (2) (15 mg/ml), UDP-GalNAc (10 eq), and hB4GalT1-Y285L mutant or bB4GalT1-Y289L mutant (%, w/w, enzyme: antibody) was incubated in a buffer containing 10 mM MnCl2 (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. Data are presented as mean ± s.d., n=2 biological replicates.