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- W1965206543 abstract "The nature of the components and some of the association forces in aggregated acetylcholinesterase, extracted from the electric organ of Electrophorus electricus, were investigated. The aggregated acetylcholinesterase (rapidly sedimenting, 70 S, and referred to as fast acetylcholinesterase) and the dissociated or “monomer” acetylcholinesterase (11.5 S and referred to as slow acetylcholinesterase) were isolated by zonal centrifugation. The fast acetylcholinesterase was further processed by gel filtration, resulting in a fast acetylcholinesterase of low specific activity and a slow acetylcholinesterase of high specific activity and a lowered sedimentation value (10.8 S). The fast acetylcholinesterase was exposed to the hydrolytic action of various enzymes (neuraminidase, hyaluronidase, alkaline phosphatase, and phospholipase A) and examined by sucrose gradient centrifugation techniques with no effect observed on the aggregation. However, phospholipases C and D and pancreatic lipase dissociated the fast acetylcholinesterase to the slow acetylcholinesterase (11.5 S). With phospholipase C, but not pancreatic lipase, the acetylcholinesterase was released from a matrix of ultraviolet absorbing, non-enzymatic material which remained in its aggregated form. With pancreatic lipase the matrix was also dissociated into a “monomer” species with a sedimentation value similar to that of the “monomer” acetylcholinesterase (resembling dissociation in high ionic strength). The hydrolytic action of the lipases did not alter the sedimentation value of the “monomer” nor its property of reversibly forming a gelatinous precipitate at pH 4.0. However, the slow acetylcholinesterase recovered from the gel column was not sensitive to the acid pH. The results indicate that the aggregated or fast acetylcholinesterase is a complex between “monomer” and a matrix of lipoproteins which, in itself, is an aggregation of molecular species similar in sedimentation value to the “monomer” acetylcholinesterase. A model is presented. Comparison between the matrix and the receptor protein is made." @default.
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- W1965206543 date "1971-10-01" @default.
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- W1965206543 title "Acetylcholinesterase Interaction with a Lipoprotein Matrix" @default.
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- W1965206543 doi "https://doi.org/10.1111/j.1432-1033.1971.tb01555.x" @default.
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