Accession Number : ADA261641


Title :   Production of Enzymatically Active Human Acetylcholinesterase in E. Coli


Descriptive Note : Midterm rept.


Corporate Author : BIOTECHNOLOGY GENERAL CORP NEW YORK


Personal Author(s) : Fischer, Meir ; Gorecki, Marian


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a261641.pdf


Report Date : 20 Dec 1992


Pagination or Media Count : 38


Abstract : Human AChE was cloned and expressed in E. coli under the regulation of the inductible lambda PL and the constitutive deo promoters. A partially purified inactive recombinant protein was recovered from inclusion bodies. After solubilization, folding and oxidation, a protein with enzymatic properties of AChE was obtained. Substitution of the C-terminal cysteine residue by serine enhanced the recovery of enzymatically active AChE. The reconstituted enzyme was indistinguishable from native AChE isolated from erythrocytes in terms of substrate specificity and inhibitor selectivity.... RAV, Human tissues, Acetylcholinesterases, Tissue cultures, Pseudocholinesterases, Recombinant DNA, Gene expression, Foreign.


Descriptors :   *ESCHERICHIA COLI , *ACETYLCHOLINESTERASE , RECOVERY , PRODUCTION , BIOLOGY , HUMANS , INCLUSIONS , GENES , INHIBITORS , ERYTHROCYTES , TERMINALS , TISSUE CULTURE , SERINE , CYSTEINE , RESIDUES , FOLDING , CULTURE , BODIES , REGULATIONS , SOLUBILITY , CLONES , OXIDATION , ENZYMES , PROTEINS , SUBSTRATES , DEOXYRIBONUCLEIC ACIDS


Subject Categories : Biochemistry
      Genetic Engineering and Molecular Biology
      Microbiology


Distribution Statement : APPROVED FOR PUBLIC RELEASE