Human erythrocyte acetylcholinesterase is an amphipathic protein whose short membrane-binding domain is removed by papain digestion.

This publication has 18 references indexed in Scilit:

• The Molecular Forms of Cholinesterase and Acetylcholinesterase in Vertebrates
  Annual Review of Neuroscience, 1982
• Molecular Forms of Acetylcholinesterase in Bovine Caudate Nucleus and Superior Cervical Ganglion: Solubility Properties and Hydrophobic Character
  Journal of Neurochemistry, 1982
• Selective labeling of the hydrophobic core of membranes with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, a carbene-generating reagent
  Biochemistry, 1981
• Gene segments encoding transmembrane carboxyl termini of immunoglobulin γ chains
  Cell, 1981
• Cell to vesicle transfer of intrinsic membrane proteins: effect of membrane fluidity
  Biochemistry, 1980
• The immunoglobulin μ chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments
  Cell, 1980
• Multiple Molecular Forms of Acetylcholinesterase from Human Erythrocyte Membranes. Interconversion and Subunit Composition of Forms Separated by Density Gradient Centrifugation in a Zonal Rotor
  European Journal of Biochemistry, 1978
• Multiple Molecular Forms of Purified Human Erythrocyte Acetylcholinesterase
  European Journal of Biochemistry, 1975
• Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agarose
  Biochemistry, 1972
• [14] Papain
  Published by Elsevier ,1970