Incubation of purified human beta 2-microglobulin (B2-m) with tissue transglutaminase (Tgase) resulted in the formation of high molecular weight polymers revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the presence of 30 mM [14C]methylamine, the polymer formation was prevented, but incorporation of methylamine into beta 2-m (equal to 1 methylamine per 1 molecule) could be observed. From the sheddings of peripheral blood mononuclear cells occurring in the presence of Tgase, it is apparent that anti-beta 2-m immunoadsorbent removed, in addition to human leukocyte antigen (HLA) and beta 2-m, some other proteins. The enzyme could incorporate [14C]methylamine into beta 2-m of the shedding cells. On addition of rabbit anti-human beta 2-m antibody, followed by fluoresceine-labeled goat anti-rabbit IgG antibody to human mononuclear blood cells, the otherwise homogeneous distribution of fluorescence turned into spots and patches on cells previously incubated with Tgase or Ca2+-ionophore A23187.
Human beta 2-microglobulin is a substrate of tissue transglutaminase: polymerization in solution and on the cell surface.
L Fésüs, A Falus, A Erdei, K Laki; Human beta 2-microglobulin is a substrate of tissue transglutaminase: polymerization in solution and on the cell surface.. J Cell Biol 1 June 1981; 89 (3): 706–710. doi: https://doi.org/10.1083/jcb.89.3.706
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