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1.
Stomatologiia (Mosk) ; 96(4): 23-27, 2017.
Artículo en Ruso | MEDLINE | ID: mdl-28858275

RESUMEN

The aim of the study was to assess the efficacy of type A Botulinus toxin (BTA) in pain release by TMJ functional pain disorders. The study included 211 patients with TMJ functional pain disorder (20.4% males and 79.6% females; mean age 45.3 years). The patients underwent clinical examination and bioelectric activity assessment of masticatory muscles by electromyography (EMG). EMG specters of 20 healthy volunteers with intact dental arches served as a control. After examination BTA was injected in muscular pain trigger points. All patients had muscular hypertonus, unilateral in 88.6% and bilateral in 11.4%. EMG showed the decrease of masticatory muscle activity on affected side to mean values of 165±20 mkV (30.0%, p<0.05) and on contralateral side to 460±31 mkV (89.6%, p>0.05). BTA injections in tensed muscles released significantly muscle-induced facial pain and improved quality of life. During 6 months follow up myofacial pain disorder relapse was seen in 3 patients. The results allow recommending BTA injection in muscular pain trigger points for treatment of myofacial pain syndrome and prolonged muscle relaxation.


Asunto(s)
Toxinas Botulínicas Tipo A/uso terapéutico , Neuralgia Facial/tratamiento farmacológico , Neuralgia Facial/etiología , Fármacos Neuromusculares/uso terapéutico , Síndrome de la Disfunción de Articulación Temporomandibular/complicaciones , Toxinas Botulínicas Tipo A/administración & dosificación , Electromiografía , Femenino , Humanos , Inyecciones Intramusculares , Masculino , Persona de Mediana Edad , Fármacos Neuromusculares/administración & dosificación , Puntos Disparadores
2.
Biofizika ; 61(2): 231-8, 2016.
Artículo en Ruso | MEDLINE | ID: mdl-27192823

RESUMEN

This work presents the results of the analysis of the fluorescence lifetime of tryptophan in three proteins: human serum albumin, bovine serum albumin and bacterial luciferase, containing 1, 2 and 7 tryptophan residues, respectively. It was shown that for all proteins fluorescence decay can be fitted by three lifetimes: τ1 = 6-7 ns, τ2 = -2,0-2,3 ns and τ3 ≤ 0,1 ns (the native state) and τ1 = 4,4-4,6 ns, τ2 = 1,7-1,8 ns and τ3 ≤ 0,1 ns (the denaturated state). It was found that spectral profiles with individual protein fluorescence lifetime have similar peak wavelength and identical half-width of the spectrum as in the native state (λ(max)τ1 = 342 nm, λ(max)τ2 = 328 nm and λ(max)τ3 = 3i5 nm), and in the denaturated state (λ(max)τ1 = 350 nm, λ(max)τ2 = 343 nm and λ(max)τ3 = 317 nm). In addition, the differences in the steady-state spectra of the studied proteins are caused by the individual ratio of lifetime contributions. The correlation between. lifetime components and a known classification of the tryptophan residues in the structure of proteins, under study was performed within the discrete states model.


Asunto(s)
Luciferasas de la Bacteria/química , Albúmina Sérica/química , Triptófano/química , Animales , Bovinos , Humanos , Conformación Proteica
3.
J Photochem Photobiol B ; 97(3): 117-22, 2009 Dec 02.
Artículo en Inglés | MEDLINE | ID: mdl-19864157

RESUMEN

The paper reports the experimental results of bioluminescence quenching in the coupled enzyme system NADH:FMN-oxidoreductase-luciferase in the presence of xanthene dyes (fluorescein, eosin Y, erythrosin B) featured by the rate constants of intersystem crossing. From the spectral data and with the help of kinetic model the rate constants of energy transfer from emitter to dye were determined (2.9 x 10(12)-6.5 x 10(13) M(-1) s(-1)) and the emitter lifetime was estimated (1.2-2.7 ns). The calculated rate constants of energy transfer in a series of xanthene molecules are higher than the diffusion-controlled constants. The rate constants of energy transfer correlate with the probability of intersystem crossing of a dye. The combined analysis of emitter fluorescence quenching and acceptor fluorescence enhancement indicates that the significant bioluminescence intensity decrease in the presence of xanthene dyes is determined by both the quenching processes via the energy transfer and the inhibition of bioluminescent reaction.


Asunto(s)
Transferencia de Energía , Colorantes Fluorescentes/química , Xantenos/química , Eosina Amarillenta-(YS)/química , Eritrosina/química , FMN Reductasa/química , FMN Reductasa/metabolismo , Fluoresceína/química , Cinética , Luciferasas/química , Luciferasas/metabolismo , Mediciones Luminiscentes
4.
J Photochem Photobiol B ; 66(3): 218-22, 2002 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-11960733

RESUMEN

The effects of potassium halides KCl, KBr and KI on NADH:FMN-oxidoreductase-luciferase bioluminescent coupled enzyme system were studied. The influence of salt additions on bioluminescence intensity and bioluminescence light yield was investigated. The inhibition and activation parameters of the salts were calculated using their dependencies on concentration of the salts. The correlation between the inhibition of bioluminescence intensity and the halide mass was demonstrated: the inhibiting ability of the salts increases with the increase of atomic weight of the anions. The inhibition parameters increase and the activation parameters decrease, accordingly.


Asunto(s)
Cationes Monovalentes/farmacología , Mediciones Luminiscentes , Photobacterium/efectos de los fármacos , Potasio/farmacología , Vibrio/efectos de los fármacos , Photobacterium/efectos de la radiación , Vibrio/efectos de la radiación
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