Some of the properties of galactosyltransferase of Golgi membrane-rich fractions from rat liver were investigated. The kinetic properties of the enzyme were determined from the initial rates of reaction under various conditions of incubation. Puromycyin, a known inhibitor of protein synthesis, was shown to inhibit the galactosyltransferase activity in vitro. The inhibition depended on the concentration of puromycin and on the duration of exposure of Golgi membranes to the drug. A number of compounds, structurally related to puromycin, were unable to produce the inhibition. A combination of the aminonucleoside and amino acid portions of the puromycin molecule was equally ineffective. Binding of puromycin to the membranes was demonstrated with [3H]puromycin. It was concluded that this binding to the membrane disrupted the enzymatic activity.
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Treloar et al. (1974) studied this question.