Posterior scissors-bite: masticatory jaw movement and muscle activity.

Scissors-bite is a malocclusion characterised by buccal inclination or buccoversion of the maxillary posterior tooth and/or linguoclination or linguoversion of the mandibular posterior tooth. This type of malocclusion causes reduced contact of the occlusal surfaces and can cause excessive vertical overlapping of the posterior teeth. This case-control study is the first to evaluate both masticatory jaw movement and masseter and temporalis muscle activity in patients with unilateral posterior scissors-bite. Jaw movement variables and surface electromyography data were recorded in 30 adult patients with unilateral posterior scissors-bite malocclusion and 18 subjects with normal occlusion in a case-control study. The chewing pattern on the scissors-bite side significantly differed from that of the non-scissors-bite side in the patients and of the right side in the normal subjects. These differences included a narrower chewing pattern (closing angle, P < 0.01; cycle width, P < 0.01), a longer closing duration (P < 0.05), a slower closing velocity (P < 0.01) and lower activities of both the temporalis (P < 0.05) and the masseter (P < 0.05) muscles on the working side. In 96% of the patients with unilateral posterior scissors-bite, the preferred chewing side was the non-scissors-bite side (P = 0.005). These findings suggest that scissors-bite malocclusion is associated with the masticatory chewing pattern and muscle activity, involving the choice of the preferred chewing side in patients with unilateral posterior scissors-bite.

Influence of maximum bite force on jaw movement during gummy jelly mastication.

It is known that maximum bite force has various influences on chewing function; however, there have not been studies in which the relationships between maximum bite force and masticatory jaw movement have been clarified. The aim of this study was to investigate the effect of maximum bite force on masticatory jaw movement in subjects with normal occlusion. Thirty young adults (22 men and 8 women; mean age, 22.6 years) with good occlusion were divided into two groups based on whether they had a relatively high or low maximum bite force according to the median. The maximum bite force was determined according to the Dental Prescale System using pressure-sensitive sheets. Jaw movement during mastication of hard gummy jelly (each 5.5 g) on the preferred chewing side was recorded using a six degrees of freedom jaw movement recording system. The motion of the lower incisal point of the mandible was computed, and the mean values of 10 cycles (cycles 2-11) were calculated. A masticatory performance test was conducted using gummy jelly. Subjects with a lower maximum bite force showed increased maximum lateral amplitude, closing distance, width and closing angle; wider masticatory jaw movement; and significantly lower masticatory performance. However, no differences in the maximum vertical or maximum anteroposterior amplitudes were observed between the groups. Although other factors, such as individual morphology, may influence masticatory jaw movement, our results suggest that subjects with a lower maximum bite force show increased lateral jaw motion during mastication.

Reactivity of soybean lipoxygenase-1 to linoleic acid entrapped in phosphatidylcholine vesicles.

The linoleic acids embedded in the SUVs of soy-PC, DMPC, and DPPC served as substrate for soybean lipoxygenase-1 (L-1). The initial velocity of the catalytic reaction and the concentration of the substrate showed a hyperbolic relation. The Km values of L-1 for the linoleic acids in soy-PC, DMPC, and DPPC vesicles were 0.07, 0.09, and 0.11 mM, respectively, being comparable with that for Tween-20 micellar linoleic acid. Soy-PC and DMPC competitively inhibited the enzyme with Ki values of 0.20 and 0.13 mM, respectively, whereas DPPC had no effect. DSC analysis revealed the phase separation of linoleic acid and DPPC in vesicles in the temperature range in which the enzyme reaction was carried out. This may account for the lack of inhibitory effect of DPPC on the enzyme. From the temperature dependence of the specific activity of the enzyme, the Ea values of the catalytic reaction were estimated to be 26.7 and 35.3 kJ.mol-1 for soy-PC and DPPC vesicles, respectively. For linoleic acid-DMPC vesicles, a two-phase temperature dependence of the activity across the transition temperature of the mixed vesicles was suggested.

Inhibition of soybean lipoxygenase-1 by n-alcohols and n-alkylthiols.

A series of n-alcohols and n-alkylthiols with carbon chains from 2 to 12 were examined for the inhibition of soybean lipoxygenase-1 (L-1). The alcohol produces a competitive inhibition, the extent of which increases with an increase in the carbon number of alkyl chain up to 8. Whereas the inhibition of the alkylthiol is noncompetitive, the extent of which is almost independent from the carbon number. From the behavior of pKi dependence on the carbon number of the alcohol, the decyl group appears to be optimum to bind to L-1. The thermodynamic analysis for the inhibition based upon van 't Hoff equation indicates positive enthalpy and entropy changes for the binding of the alcohol to the enzyme and negative enthalpy and positive to negative entropy changes for that of the alkylthiol. These observations suggest that the alcohol inhibits L-1 by binding of the hydrophobic alkyl tail to the catalytic site of the enzyme by a hydrophobic interaction. The alkylthiol inhibits by binding of the nucleophilic sulfhydryl head to a polarizable region of the enzyme and the alkyl tail to a hydrophobic region of the enzyme free from the steric hindrance as an anchor.

Assay of thiols and disulfides based on the reversibility of N-ethylmaleimide alkylation of thiols combined with electrolysis.

A simple and specific method for analyzing thiols and disulfides on the basis of the reversibility of N-ethylmaleimide (NEM) alkylation of thiols is described. When the adduct of NEM and glutathione (GSH) was electrolyzed at neutral pH, all of the GSH was recovered. When the adduct was exposed to pH 11.0 for 15 min at 30 degrees C before electrolysis, GSH was not detected. The same behavior was observed after protein thiols reacted with NEM. This pH-dependent production of thiol from the adduct was used to assay GSH and oxidized glutathione in yeast cells, to assay sulfhydryl groups and disulfide bonds in authentic proteins, and to protect thiols from oxidation during enzymatic digestion of protein. This method is useful for assay of thiols and disulfides of both small and large molecules and can be used to identify labile thiols in biological samples that are oxidized during extraction procedures.

Measurement of biological thiols and disulfides by high-performance liquid chromatography and electrochemical detection of silver mercaptide formation.

A rapid and sensitive method is described for the measurement of picomole levels of the biological thiols glutathione, cysteine, penicillamine, cysteamine, and ergothioneine by a combination of high-performance liquid chromatography and electrochemical detection (ECD). The compounds were separated isocratically on a reversed-phase C18 column by ion-pair chromatography with a mobile phase containing 5 mM acetic acid and 2.5 mM sodium 1-octanesulfonate. After chromatographic separation, the eluate was combined with silver nitrate dissolved in ammonium nitrate buffer at pH 10.5. A platinum disc electrode was used at -0.1 V vs Ag/AgCl to detect the amount of silver ions that had been consumed by the reaction with thiols. For measurement of disulfide, S-sulfonation with sodium sulfite or electroreduction were used to cleave the disulfide, and the thiol anions produced were detected by HPLC-ECD as for the reduced forms. The method was used to assay thiols and disulfides in biological materials.

Assay of biological thiols by a combination of high-performance liquid chromatography and postcolumn reaction with 6,6'-dithiodinicotinic acid.

A simple and rapid method for the determination of nanomole levels of biological thiols is described. The analysis is based on the combination of reverse-phase high-performance liquid chromatography with a postcolumn reaction with 6,6'-dithiodinicotinic acid. Thiols, including cysteine, cysteamine, thiolhistidine, homocysteine, glutathione, penicillamine, ergothioneine, and thiouracil were separated by eluting with 33 mM KH2PO4 at pH 2.2. Glutathione, cysteine, cysteamine, homocysteine, and penicillamine were quantitatively determined with detection limits of 0.1 nmol, while the quantitative detection of thiolhistidine, ergothioneine, and thiouracil was not successful. The method was applied to the assay of glutathione in human erythrocytes and Escherichia coli.