Degree Name

Master of Science (MS)

Semester of Degree Completion

1975

Thesis Director

C. Dan Foote

Abstract

Acetylcholinesterase from rat brain was studied in crude homogenates, partially purified enzyme fractions, and in synaptosomes, to observe modification of the enzyme as a consequence of the modification of the membrane containing it.

Sodium dodecyl sulfate decreases the absorbance due to particles in the homogenate. This change in absorbance was proportional to both the concentration of sodium dodecyl sulfate and the concentration of the particles. Further, sodium dodecyl sulfate caused sulfhydryl groups to appear in the crude homogenate and in partially purified enzyme fractions. Synaptosomal preparations did not give such results. At concentrations of sodium dodecyl sulfate sufficient to cause absorbance changes, and therefore to modify the membranes in the preparation, the enzyme acetylcholinesterase was completely inhibited.

A non-ionic detergent in the same range of concentrations as for sodium dodecyl sulfate, neither inhibited the enzyme nor caused any noticeable change in absorbance due to the membranous particles.

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