Effect of menthol on human temperature sensitivity

Application of 1% methol, which, along with cold, activates specific thermosensitive ionic channels, changes the number of functioning cold receptors on the skin of the forearm similarly to the cold exposure test; however, it does not affect the number of heat receptors and does not significantly change the threshold of cold sensation. Group variants of responses to menthol that indicate individual differences in the sensitivity of skin receptors to the effects of methol and cold have been found. The results obtained give grounds to suggest that, from the variant of response to menthol (a decrease, increase, or absence of changes in the number of functioning cold receptors 5 min after menthol application), it is possible to predict specific features of response to cold.     

Comparative analysis of respiratory activity in the wild type strain of <Emphasis Type="Italic">Neurospora crassa</Emphasis> and its photoreceptor complex mutants

Cell respiratory activity of protoplasts obtained from the wild type of Neurospora crassa and photoreceptor complex WCC—white collar 1 (wc-1) and white collar 2 (wc-2)—mutants of Neurospora crassa strains was investigated. Respiration inhibition by KCN in the presence of 25 mM succinate was similar in all strains and did not exceed 83–85% against control. The significant induction of KCN-resistant respiratory pathway occurred under 1% glucose oxidation in wc-1 and wc-2 mutants if compared with the wild type strains. The inhibitors of the main (cytochrome) pathway of electron transfer in mitochondria—1 mM KCN and antimycin A (4 μg/ml)—blocked the respiration rate of the protoplasts from N. crassa wild type by 75%, while the cell respiration of wc-1 and wc-2 strains was suppressed by approximately 50%. The specific inhibitor of alternative oxidase—10 mM salicylhydroxamic acid (SHAM)—in combination with the blockers of mitochondrial electron transfer chain caused the total suppression of respiratory activity of protoplasts in all studied strains. It is supposed that an increase of KCN-resistance in WCC mutants under glucose oxidation is connected with alternative oxidase activation as the result of failure in reception and signal transduction of active oxygen species.     

Biopolymer of alginate nature with a predominance of L-guluronic acid

Highly viscous polysaccharide (250–350 kDa) of an alginate nature with a predominance of α-L-guluronic acid (M/G = 0.22) was obtained from Azotobacter vinelandi. The yield of polysaccharide was 20.5 ± 0.5 g/l when cultured in a medium containing molasses at a viscosity of the cultural liquid of over 30000 cSt. The biopolymer is stable at pH 4.0–9.0 in a wide temperature range and well soluble in highly mineralized water; it retains a high viscosity level and can be used in the petroleum industry for enhanced oil recovery.     

Spinal control of afferent temperature information in the cat

The effect of picrotoxin (at sub-convulsant doses, i.v.) on the background and invoked spike activity of cat dorsal horn internerons was investigated while thermal and mechanical influences were at work on the skin receptor areas. It was found that information on skin temperature is modulated at the presynaptic level and largely mediated by competitive interaction between large and small diameter fibers.Institute of Physiology, Academy of Sciences of the Kazakh SSR, Alma Ata. Translated from Neirofiziologiya, Vol. 18, No. 6, pp. 773–779, November–December, 1986.     

Pattern of tonic activity in different groups of rabbit superior cervical ganglion neurons

Tonic activity in rabbit superior cervical ganglion neurons was investigated using intracellular recording techniques as well as changes produced when the animal breathed a gaseous mix with a raised CO₂ level. The test neurons were divided into three groups depending on the pattern of their tonic activity and reflex change. Action potentials were produced by the activity of dominant and accessory preganglionic inputs in the firing pattern of all neuronal groups, implying the existence of other types of inputs into the neurons innervating different organs. Having analyzed changes in action potential rate and EPSP in the tonic activity of neurons from different groups, it was presumed that preganglionic fibers with a similar activity pattern converge on the majority of neurons in each group.A. A. Bogomolets Institute of Physiology, Academy of Sciences of the Ukrainian SSR, Kiev. Translated from Neirofiziologiya, Vol. 19, No. 5, pp. 665–672, September–October, 1987.     

Thermodynamic and kinetic study of thermal denaturation of Kunitz soybean trypsin inhibitor by differential scanning microcalorimetry

The thermal denaturation of soybean trypsin inhibitor (Kunitz inhibitor) has been studied in pH-region from 2.0 to 11.0 by differential scanning microcalorimetry. The thermodynamic characteristics have been determined. It has been established that the denaturation transition of protein may be described by a two-state model. It has been shown, that two side hydrogen bonds between carboxylate-ion and tyrosyl and carboxylate-ion and lysyl take part in the stabilization of the inhibitor's native structure. The activation of denaturation is accompanied by cleavage of one side hydrogen bond.     

Blocking action of Nephila clavata spider toxin on ionic currents activated by glutamate and its agonists in isolated hippocampal neurons

The blocking action ofNephila clavata spider neurotoxin, or JSTX, on ionic currents activated by L-glutamate and its agonists when applied to the membrane of neurons isolated from the rat hippocampus was investigated using a concentration clamp technique. Crude JSTX venom was found to block L-glutamate-, quisqualate, and kainate-activated ionic currents induced by activating non-N-methyl-D-aspartate (non-NMDA) membrane receptors. Following the effects of JSTX, ionic currents activated by L-glutamate and its agonists declined to 34–36% of their initial value with no recovery during JSTX washout. An active fraction of JSTX at concentrations of 10^–4–10^–5 produced almost total but partially reversible blockade of ionic currents. The action of JSTX became less effective during depolarization. The concentration dependence of JSTX-induced blockade of kainate-activated ionic currents was investigated and the velocity constants of interaction between the toxin and glutamate receptors obtained. It is postulated that JSTX interacts with chemically-operated non-NMDA ionic channels, blocking their transition into a number of their possible open states.A. A. Bogomolets Institute of Physiology, Academy of Sciences of the Ukrainian SSR, Kiev. Translated from Neirofiziologiya, Vol. 21, No. 2, pp. 152–160, March–April, 1989.     

Argiopine,argiopinines, and pseudoargiopinines as glutamate receptor blockers in hippocampal neurons

A homologous set of low-molecular weight compounds selectively blocking ionic currents were purified from venom from the spiderArgiope lobata with a selective blocking action on ionic currents activated by applying glutamate and its agonist kainic acid (KA) to the membrane of neurons isolated from the rat hippocampus. Three groups of these compounds — argiopine, argiopinines, and pseudoargiopinines, produced voltage-dependent glutamate- and KA-activated ionic currents at concentrations of 10^–6-10^–4 M, interacting primarily with agonist-activated ionic channels without affecting K_d values of the agonist. The blocking action could be partially reversed by argiopine application but only slightly when argiopinines and pseudoargiopinines were used. Kinetics of toxin effects on Ka-activated ionic currents showed at least two exponential components with different time constants. Simple and reversed rate constants of interaction between toxins and ionic channels were estimated from the plot of the kinetics of ionic current blockade and recovery against toxin concentration. Argiopine, argiopinines, and pseudoargiopinines lend themselves to further research into glutamate receptors of the mammalian CNS employing electrophysiological and biochemical techniques.A. A. Bogomolets Institute of Physiology, Academy of Sciences of the Ukrainian SSR, Kiev, M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow. Translated from Neirofiziologiya, Vol. 21, No. 6, pp. 748–756, November–December, 1989.