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At least 73 records · Page 4Linked to original sources
PubMed1956

The effect of polyphosphates and magnesium on the mechanical properties of extracted muscle fibers.

Loading of extracted muscle fibers causes a small, sudden lengthening, followed by a slower, plastic extension, which is reversed only by active contraction. Polyphosphates in the presence of Mg strongly accelerate plastic extension, but elastic changes in length remain the same as during rigor. The modulus of elasticity on the average is about 6.2 x 10(7) dynes per cm.(2) This value is about 40 times larger than that of rubber, if compared on a water-free basis. Extension of muscle, therefore, is almost entirely due to plastic deformation. Mg is essential for the softening action of adenosinetriphosphate (ATP) and can produce partial relaxation in the absence of a relaxation factor. After partial removal of bound Mg, ATP causes strong contraction, but only slight softening. The same condition is produced by very low concentrations of ATP in the presence of phosphocreatine. These observations show that during contraction passive mechanical properties may remain essentially like those during rigor. The constancy of elastic extensibility distinguishes contraction produced by ATP from contraction induced by non-specific agents in various fibrous structures and caused by an increase in configurational entropy.

Adenosine Triphosphate↗
PubMed1958

The participation of phosphate in the formation of a carrier for the transport of Mg++ and Mn++ ions into yeast cells.

During the absorption of phosphate by yeast, the cells acquire the capacity to absorb Mn(++) and Mg(++), a capacity which is retained even after phosphate is no longer present in the medium. Cells pretreated with phosphate and then washed, slowly lose their ability to absorb Mn(++), the rate of loss depending on the temperature and on the metabolic state. The fermentation of sugars induces a very rapid loss of absorptive capacity, whereas the respiration of ethyl alcohol, lactate, or pyruvate has little effect. Inhibitor studies with sodium acetate, redox dyes, and arsenate, reveal parallel effects on Mn(++) absorption, and on phosphate absorption. It is concluded that the synthesis of a carrier for the transport of Mg(++) and Mn(++) involves a phosphorylation step closely coupled with reactions involved in the absorption of phosphate.

Biological Transport↗
PubMed1958

The effect of enzyme inhibitors on the resting potential and on the ion distribution of the sartorius muscle of the frog.

Isolated frog sartorii were exposed for 30 minutes to HETP-an irreversible anti-cholinesterase, and were then soaked in Ringer's at 15 degrees C. for 16 hours. At the end of the period of soaking the mean resting potential of the muscle fibers was only 29 mv. The decrease in the resting potential of the HETP-treated muscles was accompanied by a loss of potassium and a gain in sodium by the muscles. The effect of anticholinesterases on sodium extrusion was studied by incubating the muscles in a Ringer's containing half of the normal amount of sodium. The muscles respond by extruding sodium against a concentration gradient into the external medium. Sodium extrusion was blocked by prior exposure of the muscle to HETP, and reversibly blocked by exposure to physostigmine. The inhibition of sodium extrusion by physostigmine was correlated with the inhibition of the intracellular cholinesterase. Sodium extrusion was also blocked by high concentrations of 2-methyl-1,4-napthaquinone 8-sulfonic acid and by alpha-ketoglutarate, which are known to inhibit choline acetylase in vitro. But sodium extrusion was not affected by a third inhibitor of choline acetylase, phenobarbital. Sodium extrusion was unaffected by KCN and partially blocked by IAA. The IAA block was eliminated by the addition of pyruvate. It is concluded that either glycolysis or oxidative metabolism can furnish the energy needed for sodium extrusion.

Animals↗
PubMed1958

The effect of anticholinesterases on the parotid gland after parasympathetic decentralization or denervation.

Anticholinesterases (eserine, ethyl pyrophosphate, paraoxon) were injected into the parotid ducts and found to cause a secretion of saliva. After previous preganglionic, parasympathetic denervation the effects were increased above normal; this was probably due to the supersensitivity to acetylcholine which develops after the operation. After previous postganglionic, parasympathetic denervation, on the other hand, the effects were much reduced, in spite of a pronounced supersensitivity towards, for example, acetylcholine. The cause of this "subsensitivity" towards cholinesterase inhibitors is discussed.

Acetylcholine↗
PubMed1958

Potentiation of the response of frog rectus muscle to acetylcholine by isopropyl methyl phosphonofluoridate and its modification by pyridine-2-aldoxime methiodide.

Pyridine-2-aldoxime methiodide (P2AM) was used to study the relation between the recovery of cholinesterase activity of isolated frog rectus abdominis muscle and the change of isotonic response to acetylcholine after previous treatment with the anticholinesterase, isopropyl methyl phosphonofluoridate (sarin). Addition of P2AM to muscle which had been incubated with sarin produced an 88% decrease in potentiation to acetylcholine. This was accompanied by 71% and 35% recoveries of the cholinesterase activity of the intact and finely ground muscle respectively compared with controls from the contralateral muscle. Following pre-treatment with sarin, a two-hour rinsing with acetylcholine (3 mug./ml.) produced a 61% decrease in potentiation to acetylcholine accompanied by 24% and 4.5% recoveries of cholinesterase activity in intact and in ground muscle respectively. Since control experiments showed absence of uncombined sarin in the muscle after rinsing with acetylcholine solution, the results indicate a greater effectiveness of P2AM and acetylcholine in reactivating superficially situated cholinesterase of the frog rectus abdominis as compared with enzyme within the interior of the muscle.

Acetylcholine↗
PubMed1959

Oximes of alpha omega-diquaternary alkane salts as antidotes to organophosphate anticholinesterases.

Sixteen compounds of the general structure {HON: CH.C(5)H(4)N(+).[CH(2)](n).R(+)}2Br(-) have been synthesized in which the position of the oxime group in the pyridine ring, the second charged group R(+) and the number of methylene groups between the charged atoms have been varied. The rate at which these compounds reactivate cholinesterase inhibited by ethyl pyrophosphate has been studied and a number have been found which are more active than 2-hydroxyiminomethyl-N-methylpyridinium methanesulphonate. Since considerable variation in structure was found among those compounds which are better reactivators than the latter, the concept that 2-hydroxyiminomethyl-N-methylpyridinium salts are unique in their ability to fit the surface of the inhibited enzyme is no longer tenable. The reactivating power of these oximes correlated well with their ability, when given in conjunction with atropine, to save the lives of mice poisoned by ethyl pyrophosphate. The most effective compounds, NN'-trimethylenebis-(4-hydroxyiminomethylpyridinium bromide) and NN'-hexamethylenebis(2-hydroxyiminomethylpyridinium bromide), contained a further oxime group in R(+), but the second oxime group was not essential for high activity. These new oximes were also superior in saving the lives of mice poisoned with sarin (isopropyl methylphosphonofluoridate), but the improvement was not as dramatic as when the mice were poisoned with ethyl pyrophosphate. The toxicity of the compounds varied with both n and R(+) and was unrelated to the therapeutic potency.

Alkanes↗