The fast and accurate identification of nerve tracts is critical for successful nerve anastomosis. Taking advantage of differences in acetylcholinesterase content between the spinal ventral and dorsal roots, we develo...The fast and accurate identification of nerve tracts is critical for successful nerve anastomosis. Taking advantage of differences in acetylcholinesterase content between the spinal ventral and dorsal roots, we developed a novel quartz crystal microbalance method to distinguish between these nerves based on acetylcholinesterase antibody reactivity. The acetylcholinesterase antibody was immobilized on the electrode surface of a quartz crystal microbalance and reacted with the acetylcholinesterase in sample solution. The formed antigen and antibody complexes added to the mass of the electrode inducing a change in frequency of the electrode. The spinal ventral and dorsal roots were distinguished by the change in frequency. The ventral and dorsal roots were cut into 1 to 2-mm long segments and then soaked in 250 pL PBS. Acetylcholinesterase antibody was immobilized on the quartz crystal microbalance gold electrode surface. The results revealed that in 10 minutes, both spinal ventral and dorsal roots induced a frequency change; however, the frequency change induced by the ventral roots was notably higher than that induced by the dorsal roots. No change was induced by bovine serum albumin or PBS. These results clearly demonstrate that a quartz crystal microbalance sensor can be used as a rapid, highly sensitive and accurate detection tool for the quick identification of spinal nerve roots intraoperatively.展开更多
Human and bovine copper-zinc superoxide dismutases (CuZn-SOD) are not the same due to the difference of species origin, but in the primary structure of the two enzymes, 83.3％ of amino acid residue sequences are prove...Human and bovine copper-zinc superoxide dismutases (CuZn-SOD) are not the same due to the difference of species origin, but in the primary structure of the two enzymes, 83.3％ of amino acid residue sequences are proved to be identical.展开更多
基金supported by the National Natural Science Foundation of China,No. 30973058,81171694Jiangsu Province Natural Science Foundation,No. BE2010743+2 种基金Jiangsu Graduate Student Innovation Project,No.CXZZ11_0721the Program for Development of Innovative Research Team in the First Affiliated Hospital of Nanjing Medical University,No. IRT-015a Project Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions
文摘The fast and accurate identification of nerve tracts is critical for successful nerve anastomosis. Taking advantage of differences in acetylcholinesterase content between the spinal ventral and dorsal roots, we developed a novel quartz crystal microbalance method to distinguish between these nerves based on acetylcholinesterase antibody reactivity. The acetylcholinesterase antibody was immobilized on the electrode surface of a quartz crystal microbalance and reacted with the acetylcholinesterase in sample solution. The formed antigen and antibody complexes added to the mass of the electrode inducing a change in frequency of the electrode. The spinal ventral and dorsal roots were distinguished by the change in frequency. The ventral and dorsal roots were cut into 1 to 2-mm long segments and then soaked in 250 pL PBS. Acetylcholinesterase antibody was immobilized on the quartz crystal microbalance gold electrode surface. The results revealed that in 10 minutes, both spinal ventral and dorsal roots induced a frequency change; however, the frequency change induced by the ventral roots was notably higher than that induced by the dorsal roots. No change was induced by bovine serum albumin or PBS. These results clearly demonstrate that a quartz crystal microbalance sensor can be used as a rapid, highly sensitive and accurate detection tool for the quick identification of spinal nerve roots intraoperatively.
文摘Human and bovine copper-zinc superoxide dismutases (CuZn-SOD) are not the same due to the difference of species origin, but in the primary structure of the two enzymes, 83.3％ of amino acid residue sequences are proved to be identical.
