Archives of Biochemistry and Biophysics | Vol.56, Issue.2 | | Pages 469-475
Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction
Purification of human red cell cholinesterase by means of electrophoresis on paper, ultracentrifugation, and gradient exctraction is described. By these means a protein is isolated that appears to be homogeneous in gradient extraction and free electrophoresis; however, reasons are given for believing that this is not the cholinesterase protein but a major protein with which the cholinesterase is tenaciously associated.
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Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction
Purification of human red cell cholinesterase by means of electrophoresis on paper, ultracentrifugation, and gradient exctraction is described. By these means a protein is isolated that appears to be homogeneous in gradient extraction and free electrophoresis; however, reasons are given for believing that this is not the cholinesterase protein but a major protein with which the cholinesterase is tenaciously associated.
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