Acetylcholinesterase of Schistosoma mansoni. Molecular forms of the solubilized enzyme

Rebeca Tarrab-Hazdai*, Francesca Levi-Schaffer, Guadalupe Gonzales, Ruth Arnon

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Several molecular forms of acetylcholinesterase were obtained from Schistosoma mansoni homogenates by extraction in either low-salt buffer, high-salt buffer or detergent buffer. The low-salt soluble form amounts to 25% of the total activity. By constant, the extract obtained in the presence of Triton X-100 possessed almost 3-fold higher enzymatid activity, most of it (86%) being retained in the soluble extract (100 000 × g). High-salt concentration (1 M NaCl) also has a solubizing effect, but to a lesser extent (50%). Acetylcholinesterase can also be solubilized by treatment with a solution of 1% methylmannoside (40%). In the presence of non-ionic detergents, the enzyme behaves as monodisperse 8 S form. In the absence of detergent the low-salt soluble extract is polydisperse: it contains a 10 S and a 32 S component, the latter could represent high polymers. The molecular form released from tissue homogenate by treatment with α-methylmannoside is polydisperse: it contains a major 10 S and a minor 32 S component. Differences in sedimentation coefficient were observed among the enzymes extracted with detergent from the various life cycle stages of the parasite. The enzyme from the cercarial stage sediments as a single 8 S peak. The adult worm exhibits an additional acetylcholinesterase peak of 18 S representing approx. 30% of the total enzymatic activity. The molecular weight of the major 8 S species, as determined by gel filtration, is 450 000.

Original languageAmerican English
Pages (from-to)61-69
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume790
Issue number1
DOIs
StatePublished - 9 Oct 1984
Externally publishedYes

Bibliographical note

Funding Information:
We would hke to expresso ur gratitudeto Prof. Israel Silman and to Dr. Moshe Smolarskyf or theirh elpfulc ommentasn dd iscussionsT.h is work was supportedin part by Grant no. RF 79062 from the RockefelleFr oundationa nd Grant no. 281-0017fr om the Edna McConnellC lark Foundation.

Keywords

  • (S. mansoni)
  • Acetycholinesterase
  • Enzyme solubilization

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