C J Branford White

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Synaptosomes from sheep brain were incubated with Na2(35)SO4. After lysis at least twelve 35S-containing proteins were identified in the synaptosomal soluble fraction with molecular weights ranging between 13,000 and 150,000. Extraction of the particulate fraction with SDS/urea revealed a further eight [35S]proteins with 27,000-140,000 molecular weights. A(More)
noradrenaline uptake, had little effect (16% of inhibition). Transport was also dependent on aerobic metabolism: incubations with KCN ( 1 mM) or 2,4-dinitrophenol (1 mM) caused a 50% decrease. Egect of reserpine on the accumulation of I 'Hldopamine. Reserpine had no inhibitory effect on the accumulation of I 3H ldopamine after 1 day in uitro. At day 3,(More)
1. The nuclear fraction of the rat tapeworm Hymenolepis diminuta (Cestoda) contains the enzyme adenosine diphosphoribosyl transferase (ADPR-transferase). 2. The enzyme catalyzes the postsynthetic modification of some nuclear proteins by the covalent attachment of the (ADP-ribose) moiety of NAD to such proteins. 3. The reaction is dependent on DNA which(More)
Incubation of Hymenolepis diminuta with the calmodulin antagonist trifluoperazine causes lesions in the brush border of the cestode. Exposure to a phenothiazine of lower lipophilicity, trifluoperazine sulphoxide, had little effect. Characterisation of isolated brush border revealed two forms of Ca2+-ATPase which exhibited maximum activity at pH 5.5 and 7.5.(More)
Rabbit and chicken triose phosphate isomerase were labelled with iodo-(1-14C)-acetamide. The efficiencies of renaturation after denaturation in guanidinium chloride were similar to those of the unlabelled enzymes. The enzymes were immobilised to Sepharose 4B and after guanidinium treatment only immobilised monomers remained on the gel. Hybridisation studies(More)
A low molecular weight, acidic, heat stable protein has been characterised from the rat tapeworm Hymenolepis diminuta. This protein was found to activate cyclic 3', 5'-nucleotide phosphodiesterase in a Ca2+-dependent manner. The activation process was inhibited by the phenothiazine drug trifluoperazine. The biochemical properties of this protein clearly(More)