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Archives of Biochemistry and Biophysics | Vol.56, Issue.2 | | Pages 469-475

Archives of Biochemistry and Biophysics

Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction

Charles A. Zittle and Edward S. DellaMonica and Jonathan H. Custer and Ruth Krikorian  
Abstract

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.

Original Text (This is the original text for your reference.)

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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Charles A. Zittle and Edward S. DellaMonica and Jonathan H. Custer and Ruth Krikorian,.Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction. 56 (2),469-475.

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