Weise_1990_J.Protein.Chem_9_53

Reference

Title : The active site and partial sequence of cobra venom acetylcholinesterase - Weise_1990_J.Protein.Chem_9_53
Author(s) : Weise C , Kreienkamp HJ , Raba R , Aaviksaar A , Hucho F
Ref : J Protein Chem , 9 :53 , 1990
Abstract : About 30% of the primary structure of acetylcholinesterase (AchE) from the cobra Naja naja oxiana has been determined. The sequence around the serine residue labeled by diisopropylfluorophosphate (DFP) was found to be TVTLFGESAGAASVGM which is similar to the active sites of AChE from other tissues. The part of the primary structure determined shows 76% identity with AChE from Torpedo and 42% identity with the Drosophila enzyme. A surprisingly large identity (42% in the sequence determined) was found with lysophospholipase from rat.
ESTHER : Weise_1990_J.Protein.Chem_9_53
PubMedSearch : Weise_1990_J.Protein.Chem_9_53
PubMedID: 2340076

Related information

Gene_locus_frgt najna-ACHE

Citations formats

Weise C, Kreienkamp HJ, Raba R, Aaviksaar A, Hucho F (1990)
The active site and partial sequence of cobra venom acetylcholinesterase
J Protein Chem 9 :53

Weise C, Kreienkamp HJ, Raba R, Aaviksaar A, Hucho F (1990)
J Protein Chem 9 :53

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    [paper] => Weise_1990_J.Protein.Chem_9_53
    [author] => Weise C || Kreienkamp HJ || Raba R || Aaviksaar A || Hucho F
    [year] => 1990
    [title] => The active site and partial sequence of cobra venom acetylcholinesterase
    [journal] => J Protein Chem
    [volume] => 9
    [page] => 53
    [medline] => 2340076
    [abstract] => Weise_1990_J.Protein.Chem_9_53
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            [content] => About 30% of the primary structure of acetylcholinesterase (AchE) from the cobra Naja naja oxiana has been determined. The sequence around the serine residue labeled by diisopropylfluorophosphate (DFP) was found to be TVTLFGESAGAASVGM which is similar to the active sites of AChE from other tissues. The part of the primary structure determined shows 76% identity with AChE from Torpedo and 42% identity with the Drosophila enzyme. A surprisingly large identity (42% in the sequence determined) was found with lysophospholipase from rat.
        )

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