Cellular transglutaminase. Lung matrix-associated transglutaminase: characterization and activation with sulfhydryls.
作者： E T Cocuzzi , S I Chung
DOI: 10.1016/S0021-9258(19)83885-1
关键词: Stokes radius 、 Glycerol 、 Enzyme 、 Biochemistry 、 Heparin 、 Elastin 、 Sulfhydryl reagent 、 Tissue transglutaminase 、 Dithiothreitol 、 Biology 、 Cell biology 、 Molecular biology
摘要: Transglutaminase in the rat lung is tightly associated with insoluble matrix which not extractable detergent, 0.5 M NaCl, and 40% glycerol solutions. The was found to be rich heparin sulfate poor collagen, elastin, DNA. transglutaminase distinct from tissue (identifiable well-characterized guinea pig liver transglutaminase) its retention volume DEAE-Sephacel columns Kd value gel-filtration columns. enzyme activated 6-8-fold sulfhydryl reagent dithiothreitol. This activation accompanied dissociation of bound resulted changes molecular properties enzyme--increase affinity for anion-exchanger decrease Stokes radius. Addition 50 mM KSCN induced a 2-fold increase SH-dependent activity. These results suggest that agents may play role compartmental translocation lung.
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