Study on rat intestinal mucosal transglutaminase

• Main Authors: Chen, Hsi-Hsien, 陳錫賢
• Other Authors: Yu-Hui Tsai, Woan-Ruoh Lee
• Format: Others
• Language: zh-TW
• Published: 1997
• Online Access: http://ndltd.ncl.edu.tw/handle/59944619547453789707

碩士 === 台北醫學院 === 醫學研究所 === 85 === AbstractTransglutaminases (TGase) are a family of calcium- dependent enzyme catalyzing an acyltransfer reaction between peptide bound glutamine and lysine residues or primary amine. A novel calcium-independent TGase-like enzyme has been demonstrated recently in mouse intestinal mucosal cells. To purify this novel enzyme, saturated ammonium sulfate was used to fractionate the cytosol preparations. The majority of calcium- independent TGase activities was detected in the fraction precipitated at 45%~55% saturated ammonThermal stability of this novel enzyme was studied at 37(C and 50(C. The calcium- independent TGase is more stable than calcium-dependent transglutaminase at 37(C. However, activities of both enzyme were abolished at 50(C. When protease inhibitors ( PMSF, Pepstatin, Leupeptin ) were included in the homogenizing buffer, the enzyme activity was decreased as compared to that prepared in the abscense of protease inhibitors.The effect of stress and tissue repair on rat intestinal mucosal transglutaminase was studied by immunohistochemical method. The intensity of stress of transglutaminase-immunostaining increased in the intestinal mucosal tissue with the duration. To investigate whether stress causes apoptosis in duodenal mucosal villus. DNA fragmentation induced by apaptosis was assessed by in situ detection. The phenomenon of apoptotic DNA fragmentation was observed in the intestinal mucosal villi. It is suggested that the