Title : A unique hydrophobic domain of rat brain globular acetylcholinesterase for binding to cell membranes.

Pub. Date : 1992 Dec

PMID : 1461372






4 Functional Relationships(s)
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1 Labeling DS-AChE with 3-(trifluoromethyl)-3-(m-(125I)-iodophenyl) diazirine ([125I]TID) revealed, by polyacrylamide gel electrophoresis under reducing conditions, one single band of 69 kD apparent molecular mass. 3-(trifluoromethyl)-3-(m-(125i)-iodophenyl) diazirine acetylcholinesterase Rattus norvegicus
2 Labeling DS-AChE with 3-(trifluoromethyl)-3-(m-(125I)-iodophenyl) diazirine ([125I]TID) revealed, by polyacrylamide gel electrophoresis under reducing conditions, one single band of 69 kD apparent molecular mass. polyacrylamide acetylcholinesterase Rattus norvegicus
3 These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al. Salts acetylcholinesterase Rattus norvegicus
4 These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al. Disulfides acetylcholinesterase Rattus norvegicus