Chapter

Multidisciplinary Approaches to Cholinesterase Functions

pp 39-47

Molecular Organization of Recombinant Human Acetylcholinesterase

  • Baruch VelanAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
  • , Chanoch KronmanAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
  • , Moshe LeitnerAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
  • , Haim GrosfeldAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
  • , Yehuda FlashnerAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
  • , Dino MarcusAffiliated withDepartment of Biotechnology, Israel Inst. Biol. Res. Ness-Ziona
  • , Arie LazarAffiliated withDepartment of Biotechnology, Israel Inst. Biol. Res. Ness-Ziona
  • , Anat KeremAffiliated withDepartment of Biochemistry, Tel-Aviv University
  • , Shoshana Bar-NunAffiliated withDepartment of Biochemistry, Tel-Aviv University
    • , Sara CohenAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona
    • , Avigdor ShaffermanAffiliated withDepartment of Biochemistry, Israel Inst. Biol. Res. Ness-Ziona

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Abstract

Acetylcholinesterase (abbreviated AChE) occurs in multiple molecular forms in different tissues of vertebrates and invertebrates (reviewed in Massoulie and Bon, 1982; (Silman and Futerman, 1987; Chatonnet and Lockridge, 1989). This heterogeneity is generated through tissue-specific associations of various catalytic and structural subunits. Characterized catalytic subunits are divided into two major types, the T-type and the H-type, both derived from a single gene by alternative splicing Schumacher et al., 1988; Sikarov et al., 1988). Structural subunits include the collagen-like structure (Krejci et al., 1991) that allows attachment to the basal lamina and the 20kD lipid-linked hydrophobic subunit (Inestrosa et al., 1987) which is associated with the mammalian brain enzyme.