A method to study the rapid phosphorylation‐related modulation of neutral trehalase activity by temperature shifts in yeast

Abstract
Heat shock enhanced the synthesis of neutral trehalase in growing cells of Saccharomyces cerevisiae, as detected by immunological methods. The activity of the enzyme was measured in extracts obtained by two methods: cells were either harvested by filtration and subsequent disruption with glass beads at 0–4°C or immediately frozen with liquid nitrogen in the presence of Triton X-100, followed by thawing at 30°C. The first procedure yielded artificially high activities of neutral trehalase in heat-shocked cells due to rapid (S. cerevisiae by phosphorylation and dephosphorylation.