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PubMedDate not supplied

The effect of acute alloxan diabetes on the sensitivity of the rat skeletal neuromuscular junction to drugs.

Preparations from alloxan diabetic rats showed a reduced sensitivity to the neuromuscular blocking action of (+)-tubocurarine but no alteration in sensitivity to the depolarizing neuromuscular blocking drug decamethonium. Physostigmine was less effective in augmenting twitch height in preparations from alloxan diabetic rats and such preparations had a significantly lowered total cholinesterase activity compared with control preparations. An additional observation was a reduction in the effectiveness of the pre-junctionally active agent beta-bungarotoxin in producing neuromuscular blockade in physostigmine-treated preparations from alloxan diabetic rats. All the changes produced by alloxan administration were prevented by treatment with insulin.

Alloxan↗
PubMed1975

Central nervous system effects of bupivacaine.

The central nervous system and concurrent cardiovascular effects of bupivacaine infusion were studied in cats. It was possible to block cortical E.E.G. desynchronization resulting from a sensory stimulus with bupivacaine. The earliest subcortical change that occurred was rhythmic activity in the amygdala and later in the hippocampus. Occasionally, this activity appeared simultaneously in both these sites. Diazepam pretreatment raised the seizure threshold of bupivacaine. Diazepam was also effective in terminating established seizure activity resulting from bupivacaine. All animals pretreated with diazepam (Valium) or diazepam solvent developed cardiac dysrhythmias durind bupivacaine infusion. The possible clinical significance of the interaction of bupivacaine and diazepam solvent is considered.

Amygdala↗
PubMed2002

Effects of membranotropic agents on mono- and multilayer structures of dipalmitoylphosphatidylcholine.

We have studied the action of some membranotropic agents (MTAs) on the parameters of mono- and multilayers of dipalmitoylphosphatidylcholine (DPPC). The MTAs used included an antimicrobial drug, decamethoxinum, the model amphiphilic agent stearoyl-L-alpha-alanine, and cholesterol as a reference substance. Using differential scanning calorimetry and the Langmuir monolayer technique, we measured the temperature and enthalpy of the main phase transition of DPPC, the mean molecular area, the collapse pressure and the free energy of the mixed monolayers of DPPC and MTA. A good correlation has been obtained between the structure of the MTA used and changes in the parameters of both mono- and multilayers. Thus, for cholesterol, its well-known condensing effect in the L alpha phase correlates with its behavior in the mixed monolayers. The disturbing action of decamethoxinum (depression of the phase transition in DPPC multilayers and relatively high free energy of mixing in monolayers) is presumably connected with interaction of its charged ammonium moieties with polar phospholipid heads. At the same time, stearoyl-L-alpha- alpha-alanine condensed the lipid layers and increased the melting point of DPPC, owing to its interaction with both polar and non-polar lipid moieties. One can conclude that the three MTAs used can really be considered as representative examples of three different types of behavior in mono- and multilayers.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1978

The acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators as an electrostatic effect.

1. In order to check our hypothesis of the electrostatic nature of the acceleration of methanesulfonylation of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) with cationic accelerators, equations were solved for methane-sulfonylation with two accelerators and the reaction was studied in the presence of some single accelerators, including the sodium cation, and in the presence of two acclerators simultaneously. 2. The second-order rate constants for methanesulfonylation of the complexes between the enzyme and accelerators decamethonium, tetraethylammonium and tetramethylammonium are 90, 88 and 17 1 - mol-1 - s-1, respectively, which corresponds to a maximal acceleration of 29, 28 and 5.5 times, respectively. The dissociation constants for the binding of these accelerators to the enzyme, obtained from our acceleration experiments, are 3.7 - 10(-6), 3.2 - 10(-4) and 1.4 - 10(-3) M, respectively. These values are in good agreement with the dissociation constants of these ligands as inhibitors of acetylcholinesterase. It is interesting to note that the sodium cation also accelerates the methane-sulfonylation up to around three times, the corresponding second-order rate constant and the dissociation constant being 10 1 - mol-1 - s-1 and 1.3 M, respectively. 3. All tested cations compete in the acceleration with each other; they seem to accelerate the reaction in the same way and from the same site, the catalytic anionic site. 4. These findings confirm the hypothesis of the electrostatic nature of acceleration.

Acetylcholinesterase↗