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Molecular Polymorphism of Head Acetylcholinesterase from Adult Houseflies ( Musca domestica L.)
Author(s) -
Fournier D.,
Cuany A.,
Bride J. M.,
Bergé J. B.
Publication year - 1987
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1987.tb01014.x
Subject(s) - housefly , acetylcholinesterase , chemistry , musca , monomer , chromatography , molecular mass , polyacrylamide gel electrophoresis , biochemistry , electrophoresis , gel electrophoresis , membrane , amphiphile , enzyme , biology , polymer , organic chemistry , copolymer , botany , larva
Acetylcholinesterase (AChE) from housefly heads was purified by affinity chromatography. Three different native forms were separated by electrophoresis on poly‐acrylamide gradient gels; Two hydrophilic forms presented apparent molecular weights of 75,000 (AChE1) and 150,000 (AChE2). A third component (AChE3) had a migration that depended on the nature and concentration of detergents. In the presence of sodium deoxycholate in the gel, AChE3 showed an apparent molecular weight very close to that of AChE2. Among the three forms, AChE3 was the only one found in purified membranes. The relationships among the various forms were investigated using reduction with 2‐mercaptoethanol or proteolytic treatments. Such digestion converted purified AChE3 into AChE2 and AChE1, and reduction of AChE3 and AChE2 by 2‐mercaptoethanol gave AChE1, in both cases with a significant loss of activity. These data indicate that the three forms of purified AChE may be classified as an active hydrophilic monomeric unit (G 1 ) plus hydrophilic and amphiphilic dimers. These two components were termed G 2s and G 2m , where “s” refers to soluble and “m” to membrane bound.).