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PubMed1980

Decamethonium and hexamethonium block K+ channels of sarcoplasmic reticulum.

The sarcoplasmic reticulum membrane (SR) of skeletal muscle contains cation-selective channels which have been detected by isotope fluxes in fragmented SR vesicles, fluorimetric dyes and direct incorporation of SR vesicles to planar phospholipid bilayers. SR channels incorporated in bilayers have a single open-state conductance of 140 pS in 0.1 MK+ (refs 4,5). We have previously reported blockade of the SR channel by Cs+, a low-affinity blocker with a zero-voltage dissociation constant of 40 mM (ref. 6). We showed that increasing Cs+ concentrations reduced the open-channel conductance, increased the mean open time and conferred voltage dependence on the open-state conductance. Here we report on the blockade induced by the cholinergic drugs decamethonium and hexamethonium on the SR channel. Although blockade by hexamethonium is similar to that of Cs+, decamethonium blocks with a much higher affinity and induces flickering events which are probably due to the interaction of single drug molecules with the open state.

Decamethonium Compounds↗
PubMed1981

Charge screening by cations affects the conformation of the mitochondrial inner membrane. A study of exogenous MAD(P)H oxidation in plant mitochondria.

Cations caused a decrease in the apparent Km and an increase in the Vmax. for the oxidation of exogenous NADH by both Jerusalem-artichoke (Helianthus tuberosus) and Arum maculatum (cuckoo-pint) mitochondria prepared and suspended in a low-cation medium (approximately or equal to 1 mM-K+). In Arum mitochondria the addition of cations caused a much greater stimulation of the oxidation of NAD(P)H via the cytochrome oxidase pathway than via the alternative, antimycin-insensitive, pathway. This shows that cations affected a rate-limiting step in the electron-transport chain at or beyond ubiquinone, the branch-point of electron transport in plant mitochondria. The effects were only dependent on the valency of the cation (efficiency C3+ greater than C2+ greater than C+) and not on its chemical nature, which is consistent with the theory of the diffuse layer. The results are interpreted to show that the screening of fixed negative membrane changes on lipids and protein complexes causes a conformational change in the mitochondrial inner membrane, leading to a change in a rate-limiting step of NAD(P)H oxidation. More specifically, it is proposed that screening removes electrostatic restrictions on lateral diffusion and thus accelerates diffusion-limited steps in electron transport.

Decamethonium Compounds↗
PubMed1986

Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.

Optimal design of experiments as well as proper analysis of data are dependent on knowledge of the experimental error. A detailed analysis of the error structure of kinetic data obtained with acetylcholinesterase showed conclusively that the classical assumptions of constant absolute or constant relative error are inadequate for the dependent variable (velocity). The best mathematical models for the experimental error involved the substrate and inhibitor concentrations and reflected the rate law for the initial velocity. Data obtained with other enzymes displayed similar relationships between experimental error and the independent variables. The new empirical error functions were shown superior to previously used models when utilized in weighted non-linear-regression analysis of kinetic data. The results suggest that, in the spectrophotometric assays used in the present study, the observed experimental variance is primarily due to errors in determination of the concentrations of substrate and inhibitor and not to error in measuring the velocity.

Acetylcholine↗
PubMed1999

Physicochemical and immunological studies of the N-terminal domain of the Torpedo acetylcholine receptor alpha-subunit expressed in Escherichia coli.

The nicotinic acetylcholine receptor (AChR) from the electric organ of Torpedo species is an oligomeric protein composed of alpha2 beta gamma delta subunits. Although much is known about its tertiary and quaternary structure, the conformation of the large extracellular domains of each of the subunits has not been analysed in detail. In order to obtain information about the spatial structure of the extracellular domain, we have expressed the N-terminal fragment 1-209 of the Torpedo californica AChR alpha-subunit in Escherichia coli. Two vectors coding for a (His)6 tag, either preceding or following the 1-209 sequence, were used and the recombinant proteins obtained (designated alpha1-209pET and alpha1-209pQE, respectively) were purified by affinity chromatography on a Ni2+-agarose column. The chemical structure of both proteins was verified by Edman degradation and mass spectrometry. The proteins were soluble in aqueous buffers but to make possible a comparison with the whole AChR or its isolated subunits, the recombinant proteins were analyzed both in aqueous solution and with the addition of detergents. The two proteins bound [125I]alpha-bungarotoxin with equal potency (KD approximately 130 nm, Bmax approximately 10 nmol.mg-1). Both were shown to interact with several monoclonal antibodies raised against purified Torpedo AChR. The circular dichroism (CD) spectra of the two proteins in aqueous solution revealed predominantly beta-structure (50-56%), the fraction of alpha-helices amounting to 32-35%. Nonionic (beta-octylglucoside) and zwitterionic (CHAPS) detergents did not appreciably change the CD spectra, while the addition of SDS or trifluoroethanol decreased the percentage of beta-structure or increased the alpha-helicity, respectively. The predominance of beta-structure is in accord with recent data on the N-terminal domain of the mouse muscle AChR alpha-subunit expressed in the mammalian cells [West et al. (1997) J. Biol. Chem. 272, 25 468]. Thus, expression in E. coli provides milligram amounts of the protein that retains several structural characteristics of the N-terminal domain of the Torpedo AChR alpha-subunit and appears to share with the latter a similar secondary structure. The expression of recombinant polypeptides representing functional domains of the AChR provides an essential first step towards a more detailed structural analysis.

Amino Acid Sequence↗
PubMed1970

Use of a snake venom toxin to characterize the cholinergic receptor protein.

alpha-Bungarotoxin, a polypeptide of mol wt 8000 purified from the venom of Bungarus multicinctus, blocks irreversibly and specifically the excitation by cholinergic agonists on the isolated electroplax and on purified membrane fragments in vitro. The toxin also blocks the in vitro binding of decamethonium to a protein recently isolated from electric tissue. This observation strengthens our earlier conclusion that this protein is the cholinergic receptor macromolecule.

Animals↗
PubMed1971

Binding sites for cholinergic ligands in a particulate fraction of Electrophorus electroplax.

The binding of four radioactive cholinergic ligands to a particulate fraction of Electrophorus electricus electroplax was investigated by equilibrium dialysis and found to be reversible. A single site (concentration, 0.02-0.03 nmol/g electroplax) that bound muscarone and nicotine was found to be on a phospholipoprotein; it is suggested that this is the acetylcholine receptor. Four binding sites for decamethonium were found; the highest-affinity site (0.03 nmol/g) may be the same one that binds muscarone and nicotine, both because of the chemical nature of the binding macromolecule and because decamethonium competes with muscarone and nicotine in binding. Dimethylcurare bound to three sites. The lower-affinity sites appeared to be on different macromolecules.When binding of the four cholinergic ligands (at 0.01 muM) to 28 arbitrarily selected proteins was determined, it was concluded that muscarone would be the most specific for the acetylcholine receptor, in that it bound to none of the 28 proteins tested; nicotine bound to one, dimethylcurare to two, and decamethonium to ten of the proteins. Nicotine or muscarone appear to be the ligands of choice in studying binding to the acetylcholine receptor; decamethonium appears to have inadequate specificity.

Acetylcholine↗