Signorini M, Caselli L, Lanzara V, Ferrari C, Melandri P, Bergamini C M
Department of Biochemistry and Molecular Biology, University of Ferrara, Italy.
Biol Chem Hoppe Seyler. 1996 Mar;377(3):167-73. doi: 10.1515/bchm3.1996.377.3.167.
Homogenates of Yoshida hepatoma cells, cultured as ascite suspension in vivo, display significant transglutaminase activity in both the cytosolic and the particulate fraction. The enzyme, however, is predominantly membrane-bound. Transglutaminase was solubilized from the membranes either by extraction with detergents or treatment with neutralized hydroxylamine or proteinases. We observed similar molecular weight under denaturing conditions, catalytic and immunologic properties for purified cytosolic and solubilized transglutaminase, and identity of the limited proteolytic maps. These results suggest that transglutaminase isoforms actually consist of the same protein undergoing translocation by unknown mechanisms.
