The localization of honey bee thorax trehalase

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Abstract
Differential and sucrose gradient centrifugation of honey bee [Cipis mellifera] thoraces, disrupted by gentle methods and using mannitol-triethanolamine-EDTA buffer at pH 6.5, showed that in the honey bee thorax 92-94.8% of the rehalase was mitochondrial. Since only 92-95% of the cytochrome c oxidase, a known mitochondrial enzyme, was found in the mitochondrial fraction honey bee trehalase is probably totally mitochondrial. Significant amounts of microsomal or soluble trehalase were formed only by harsh methods of purified whole mitochondria. They seem to be artifacts of the isolation procedure. Studies (using marker enzymes) with purified intact mitochondria dispersed by various chemical, enzymatic and physical methods showed that the trehalase in the mitochondria was membrane bound to either the outside of the inner membrane or to 1 of the sides of the outer membrane.

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