1. Biochemical evidence of glycosylation of CaV3.2 channels.
Biochemical evidence of glycosylation of CaV3.2 channels. Immunoblotting with FLAG antibody reveals a shift in apparent molecular weight of NH2-terminal fragment of CaV3.2 channel (bottom arrow) but not full channel (top arrow). Note that treatment with PNGase-F and Endo F1 but not Endo F2 and Endo F3 caused an obvious change in mobility of FLAG-labeled NH2-terminal fragment of CaV3.2 from ~60 to 50 KDa. Using mass spectrometry, we confirmed that the deglycosylated NH2-terminal fragment of CaV3.2 channels recognized by FLAG antibodies contains most of the repeat I of CaV3.2 channel (data not shown). N-term., NH2-terminal.
Peihan Orestes et al. Diabetes 2013;62:
©2013 by American Diabetes Association