Characterization of antibody against human liver guanase by immunoblotting and immunohistochemical staining of human liver guanase by a direct labeling antibody-enzyme methodS Ito, A Iwasaki, J Syundo, Y Tamura, S Kishi, H Mori, K Ii, Y Matsuda and N Katsunuma Second Department of Internal Medicine, School of Medicine, University of Tokushima, Japan. Human liver guanase was purified and a specific antibody against it was raised in rabbits. The antiserum formed a single precipitin line with human liver extract, and also completely inhibited the activity of the liver enzyme. An immunoblotting study showed that the antibody bound specifically to one band of protein with guanase activity and not to other proteins. Therefore, we concluded that this antiserum against the liver enzyme was suitable for use in immunohistochemical demonstration of guanase. In tissue sections, the immunohistochemical reaction with this antibody was positive in the same locations as the histochemical guanase reaction with DAB (3,3'-diaminobenzidine tetrahydrochloride).
Volume 37,
Issue 5,
pp. 611-615,
05/01/1989
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H. Kuwahara, N. Araki, K. Makino, N. Masuko, S. Honda, K. Kaibuchi, K. Fukunaga, E. Miyamoto, M. Ogawa, and H. Saya A Novel NE-dlg/SAP102-associated Protein, p51-nedasin, Related to the Amidohydrolase Superfamily, Interferes with the Association between NE-dlg/SAP102 and N-Methyl-D-aspartate Receptor J. Biol. Chem., November 5, 1999; 274(45): 32204 - 32214. [Abstract] [Full Text] [PDF] |
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G. Yuan, J. C. Bin, D. J. McKay, and F. F. Snyder Cloning and Characterization of Human Guanine Deaminase. PURIFICATION AND PARTIAL AMINO ACID SEQUENCE OF THE MOUSE PROTEIN J. Biol. Chem., March 19, 1999; 274(12): 8175 - 8180. [Abstract] [Full Text] [PDF] |
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