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1.
IEEE J Biomed Health Inform ; 27(5): 2288-2295, 2023 05.
Artigo em Inglês | MEDLINE | ID: mdl-34665750

RESUMO

Restrictive public health measures such as isolation and quarantine have been used to reduce the pandemic virus's transmission. With no proper treatment, older adults have been specifically advised to stay home, given their vulnerability to COVID-19. This pandemic has created an increasing need for new and innovative assistive technologies capable of easing the lives of people with special needs. Smart home systems have become widely popular in providing such assistive services to isolated older adults. These systems can provide better services to assist older people if it anticipates what activities inhabitants will perform ahead of time. For example, a smart home can prompt inhabitants to initiate essential activities like taking medicine using activity prediction. This paper proposes a multi-task activity prediction system that jointly predicts labels, locations, and starting times of future activities. The observed sequence of previous activities characterizes future activities. We use body activity information from wearable sensors and motion information from passive environmental sensors to sense activities of daily living of older adults. The activity prediction system consists of recurrent neural networks to capture temporal dependencies. This work also carries out several experiments on collected and existing real datasets to evaluate the system's performance.


Assuntos
COVID-19 , Tecnologia Assistiva , Humanos , Idoso , Atividades Cotidianas
2.
IEEE J Biomed Health Inform ; 26(11): 5494-5505, 2022 11.
Artigo em Inglês | MEDLINE | ID: mdl-36048978

RESUMO

Epilepsy is a severe threat to society due to the treatment time, cost, and unpredictable nature of the disease, thereby imposing an urgent need for intelligent analysis. Electroencephalogram (EEG) is a commonly deployed test for detecting epilepsy that analyses the electrical activity of an individual's brain. This work proposes an optimized deep sequential model to improve the seizure classification performance based on a hybrid feature set derived from EEG signals. A novel hybridized Battle Royale Search and Rescue optimization (BRRO) algorithm is proposed for optimizing a deep learning (DL) model. Also, the proposed hybrid feature set utilizes empirical mode decomposition, variational mode decomposition, and empirical wavelet transform to capture the temporal property of the data set. The proposed method is validated using publicly available data sets. The results manifest that the proposed optimized algorithm provides better results than the other alternatives.


Assuntos
Epilepsia , Trabalho de Resgate , Humanos , Convulsões/diagnóstico por imagem , Epilepsia/diagnóstico por imagem , Eletroencefalografia/métodos , Análise de Ondaletas , Algoritmos , Processamento de Sinais Assistido por Computador
3.
Neural Process Lett ; 53(6): 3981-4010, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34305439

RESUMO

Training a machine learning model on the data sets with missing labels is a challenging task. Not all models can handle the problem of missing labels. However, if these data sets are further corrupted with label noise, it becomes even more challenging to train a machine learning model on such data sets. We propose to use a transductive support vector machine (TSVM) for semi-supervised learning in this situation. We make this model robust to label noise by using a truncated pinball loss function with it. We name our approach, pin ¯ -TSVM. We provide both the primal and the dual formulations of the obtained robust TSVM for linear and non-linear kernels. We also perform experiments on synthetic and real-world data sets to prove the superior robustness of our model as compared to the existing approaches. To this end, we use small as well as large-scale data sets to perform the experiments. We show that the model is capable of training in the presence of label noise and finding the missing labels of the data samples. We use this property of pin ¯ -TSVM to detect the coronavirus patients based on their chest X-ray images.

4.
J Phys Condens Matter ; 28(37): 376001, 2016 09 21.
Artigo em Inglês | MEDLINE | ID: mdl-27419361

RESUMO

Magnetoresistance (MR), thermo power, magnetization and Hall effect measurements have been performed on Co-doped Bi2Se3 topological insulators. The undoped sample shows that the maximum MR as a destructive interference due to a π-Berry phase leads to a decrease of MR. As the Co is doped, the linearity in MR is increased. The observed MR of Bi2Se3 can be explained with the classical model. The low temperature MR behavior of Co doped samples cannot be explained with the same model, but can be explained with the quantum linear MR model. Magnetization behavior indicates the establishment of ferromagnetic ordering with Co doping. Hall effect data also supports the establishment of ferromagnetic ordering in Co-doped Bi2Se3 samples by showing the anomalous Hall effect. Furthermore, when spectral weight suppression is insignificant, Bi2Se3 behaves as a dilute magnetic semiconductor. Moreover, the maximum power factor is observed when time reversal symmetry (TRS) is maintained. As the TRS is broken the power factor value is decreased, which indicates that with the rise of Dirac cone above the Fermi level the anomalous Hall effect and linearity in MR increase and the power factor decreases.

5.
Andrology ; 2(6): 809-18, 2014 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-25269421

RESUMO

The aim of this review was to provide current scenario linking obesity and male fertility. Obesity has been linked to male fertility because of lifestyle changes, internal hormonal environment alterations, and sperm genetic factors. A few studies assessing the impact of obesity on sperm genetic factor have been published, but they did not lead to a strong consensus. Our objective was to explore further the relationship between sperm genetic factor and obesity. There are emerging facts that obesity negatively affects male reproductive potential not only by reducing sperm quality, but in particular it alters the physical and molecular structure of germ cells in the testes and ultimately affects the maturity and function of sperm cells. Inhibition of microRNA in the male pronucleus of fertilized zygotes produces offspring of phenotypes of variable severity depending on miRNAs ratios. Hence, these RNAs have a role in the oocyte development during fertilization and in embryo development, fetal survival, and offspring phenotype. It has been reported that the miRNA profile is altered in spermatozoa of obese males, however, the impact of these changes in fertilization and embryo health remains as yet not known.


Assuntos
Infertilidade Masculina/complicações , Obesidade/complicações , Adipocinas/fisiologia , Citocinas/fisiologia , Humanos , Infertilidade Masculina/fisiopatologia , Estilo de Vida , Masculino , Obesidade/genética , Obesidade/fisiopatologia
6.
J Med Phys ; 33(3): 119-26, 2008 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-19893702

RESUMO

The objective of developing this software is to achieve auto-segmentation and tissue characterization. Therefore, the present algorithm has been designed and developed for analysis of medical images based on hybridization of syntactic and statistical approaches, using artificial neural network (ANN). This algorithm performs segmentation and classification as is done in human vision system, which recognizes objects; perceives depth; identifies different textures, curved surfaces, or a surface inclination by texture information and brightness. The analysis of medical image is directly based on four steps: 1) image filtering, 2) segmentation, 3) feature extraction, and 4) analysis of extracted features by pattern recognition system or classifier. In this paper, an attempt has been made to present an approach for soft tissue characterization utilizing texture-primitive features with ANN as segmentation and classifier tool. The present approach directly combines second, third, and fourth steps into one algorithm. This is a semisupervised approach in which supervision is involved only at the level of defining texture-primitive cell; afterwards, algorithm itself scans the whole image and performs the segmentation and classification in unsupervised mode. The algorithm was first tested on Markov textures, and the success rate achieved in classification was 100%; further, the algorithm was able to give results on the test images impregnated with distorted Markov texture cell. In addition to this, the output also indicated the level of distortion in distorted Markov texture cell as compared to standard Markov texture cell. Finally, algorithm was applied to selected medical images for segmentation and classification. Results were in agreement with those with manual segmentation and were clinically correlated.

7.
Artigo em Inglês | MEDLINE | ID: mdl-16307903

RESUMO

Ternary copper(II) complexes involving polypyridyl ligands in the coordination sphere of composition [Cu(tpy)(phen)](ClO4)2 (1), [Cu(tpy)(bipy)](ClO4)2 (2), [Cu(tptz)(phen)](ClO4)2 (3) and [Cu(tptz)(bipy)](BF4)2 (4) where tpy = 2,2':6',2''-terpyridine, tptz = 2,4,6-tri(2-pyridyl)-1,3,5-triazine, phen = 1,10-phenanthroline and bipy = 2,2'-bipyridine have been synthesized and characterized by elemental analysis, magnetic susceptibility, X-band e.p.r. spectroscopy and electronic spectroscopy. Single crystal X-ray of (1) has revealed the presence of a distorted square pyramidal geometry in the complex. Magnetic susceptibility measurements at room temperature were in the range of 1.77-1.81 BM. SOD and antimicrobial activities of these complexes were also measured. Crystal data of (1): P-1, a = 9.3010(7) A, b = 9.7900(6) A, c = 16.4620(6) A, Vc = 1342.73(14) A3, Z = 4. The bond distance of CuN in square base is 2+/-0.04 A.


Assuntos
Antibacterianos/química , Antifúngicos/química , Cobre/química , Compostos Organometálicos/química , Antibacterianos/síntese química , Antibacterianos/farmacologia , Antifúngicos/síntese química , Antifúngicos/farmacologia , Bactérias/efeitos dos fármacos , Cristalografia por Raios X , Fungos/efeitos dos fármacos , Ligantes , Microscopia Eletrônica , Estrutura Molecular , Compostos Organometálicos/síntese química , Compostos Organometálicos/farmacologia , Superóxido Dismutase/química
8.
Spectrochim Acta A Mol Biomol Spectrosc ; 62(1-3): 261-8, 2005 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-16257723

RESUMO

Two new mixed ligand copper(II) complexes with diethylenetriamine, 2,2'-bipyridine and 1,10-phenanthroline have been synthesized. The crystal and molecular structures of [Cu(dien)(phen)](ClO(4))(2) and [Cu(dien)(bipy)](BF(4))(2) (dien=diethylenetriamine, phen=1,10-phenanthroline, bipy=2,2'-bipyridine) were determined by X-ray crystallography from single crystal data. These two complexes have similar structures. The EPR spectral data also suggest that these complexes have distorted square pyramidal geometry about copper(II). Anti-microbial and superoxide dismutase activities of these complexes have also been measured. They show the higher SOD activity than the corresponding simple Cu(II)-dien/Cu(II)-PMDT (PMDT=N,N,N',N',N''-pentamethyldiethylenetriamine) complexes because of a strong axial bond of one of the nitrogen atoms of the alpha-diimine. Both the complexes have been found to cleave plasmid DNA in the presence of co-reductants such as ascorbic acid and glutathione.


Assuntos
Cobre/química , Fenantrolinas/química , Poliaminas/química , Antibacterianos/farmacologia , Cobre/farmacologia , Cristalografia por Raios X , Espectroscopia de Ressonância de Spin Eletrônica , Escherichia coli/efeitos dos fármacos , Cinética , Ligantes , Testes de Sensibilidade Microbiana , Modelos Moleculares , Conformação Molecular , Fenantrolinas/farmacologia , Plasmídeos/metabolismo , Poliaminas/farmacologia , Proteus/efeitos dos fármacos , Pseudomonas/efeitos dos fármacos , Salmonella/efeitos dos fármacos , Staphylococcus/efeitos dos fármacos , Superóxido Dismutase/metabolismo
9.
Spectrochim Acta A Mol Biomol Spectrosc ; 61(11-12): 2603-10, 2005 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-16043054

RESUMO

X-band electron spin resonance (ESR) and UV-vis spectra of a homobinuclear [(Bipy)2Cu-E-Im-Cu(Bipy)2](BF4)3 and a heterobinuclear [(Bipy)2Cu-E-Im-Zn(Bipy)2](BF4)3 complexes, E-Im=2-ethylimidazolate ion have been described as possible models for superoxide dismutase (SOD). Magnetic moment and ESR spectral measurements of the homobinuclear complex have shown an antiferromagnetic exchange interaction. From pH-dependent ESR and UV-vis spectral measurements studies, these complexes have been found to be stable over 8.5-10.5 pH range. These complexes catalyze the dismutation of superoxide (O2-) at biological pH. All the observations indicate that these complexes act as good possible models for superoxide dismutase.


Assuntos
Materiais Biomiméticos/síntese química , Materiais Biomiméticos/farmacologia , Cobre/química , Compostos Organometálicos/química , Zinco/química , Antibacterianos/síntese química , Antibacterianos/química , Antibacterianos/farmacologia , Materiais Biomiméticos/química , Cor , Dimetil Sulfóxido , Espectroscopia de Ressonância de Spin Eletrônica , Concentração de Íons de Hidrogênio , Magnetismo , Estrutura Molecular , Proteus vulgaris/efeitos dos fármacos , Soluções/química , Espectrofotometria , Superóxido Dismutase/metabolismo , Superóxidos/química , Superóxidos/metabolismo
10.
Artigo em Inglês | MEDLINE | ID: mdl-15863062

RESUMO

X-band E.S.R., magnetic and electronic spectra of some imidazolate-bridged homometallic complexes [(en)2Cu-R-Im-Cu(en)2](ClO4)3 where en, ethylenediamine; R-ImH, R = H imidazole (ImH); if R = CH3, 2-methylimidazole (M-ImH) and if R = C2H5, 2-ethylimidazole (E-ImH), and mononuclear complexes [(en)Cu-dien](ClO4)2 and [(en)Cu-PMDT](ClO4)2 where dien, diethylenetriamine; PMDT, pentamethyldiethylenetriamine have been described. Superoxide dismutase (SOD) activity has also been measured and compared with earlier reported complexes. In frozen solution at 77 K, the spectra show axial symmetry with a d(x2-y2) ground state. Difference in lambda(max) between mononuclear and binuclear complexes was found to be approximately 65-75 nm. Magnetic susceptibility and E.S.R. spectral measurements for all these binuclear complexes revealed that the copper(II) ions are involved in antiferromagnetic exchange interactions propagated by the imidazolate bridge.


Assuntos
Cobre/química , Espectroscopia de Ressonância de Spin Eletrônica/métodos , Etilenodiaminas/química , Imidazóis/química , Compostos Organometálicos/química , Superóxido Dismutase/química , Sítios de Ligação , Campos Eletromagnéticos , Elétrons , Concentração de Íons de Hidrogênio , Concentração Inibidora 50 , Ligantes , Magnetismo , Modelos Químicos , Conformação Molecular , Espectrofotometria , Superóxidos/química , Temperatura
11.
J Inorg Biochem ; 99(2): 651-63, 2005 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-15621300

RESUMO

Four imidazolate-bridged binuclear copper(II)-copper(II) and copper(II)-zinc(II) complexes viz., [(Bipy)(2)Cu-Im-Cu(Bipy)(2)](ClO(4))(3).CH(3)OH, [(Phen)(2)Cu-Im-Cu(Phen)(2)](BF(4))(3).2CH(3)OH, [(Bipy)(2)Cu-Im-Zn(Bipy)(2)](BF(4))(3), and [(Phen)(2)Cu-Im-Zn(Phen)(2)](BF(4))(3), (Bipy=2,2'-Bipyridyl, Phen=1-10-Phenanthroline and Im=imidazolate ion) were synthesized as a possible models for superoxide dismutase (SOD). Complex [(Bipy)(2)Cu-Im-Cu(Bipy)(2)](ClO(4))(3).CH(3)OH has been structurally characterized. This complex crystallizes in the triclinic space group P1, with the unit parameters a=8.88(5) A, b=13.79(17) A, c=20.18(18) A, alpha=76.424(8)(o), beta=85.888(6)(o), gamma=82.213(7). The metal-nitrogen bond length from 1.972-2.273 A and the distance Cu-Cu is 5.92 A. The five-coordinate geometry about the copper(II) ion is square pyramidal. Magnetic moment and electron paramagnetic resonance (e.p.r.) spectral measurements of the homobinuclear complexes have shown an antiferromagnetic exchange interaction. From the e.p.r. and UV-Vis spectral measurement studies, these complexes have been found to be stable (pH 8.5-10.5 for 1, 10.5 for 2,3 and 8.5 for 4). These complexes catalyse the dismutation of superoxide radical (O(2)(-)) at biological pH. All the observations indicate that these complexes act as good possible models for superoxide dismutase.


Assuntos
Cobre/química , Compostos Organometálicos/química , Compostos Organometálicos/síntese química , Superóxido Dismutase/química , Zinco/química , Animais , Antibacterianos/síntese química , Antibacterianos/química , Antibacterianos/farmacologia , Domínio Catalítico , Bovinos , Cristalografia por Raios X , Espectroscopia de Ressonância de Spin Eletrônica , Técnicas In Vitro , Modelos Químicos , Estrutura Molecular , Compostos Organometálicos/farmacologia , Espectrometria de Massas de Bombardeamento Rápido de Átomos , Espectrofotometria
12.
Spectrochim Acta A Mol Biomol Spectrosc ; 61(1-2): 287-97, 2005 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-15556452

RESUMO

The imidazolate-bridged binuclear copper(II)-copper(II) complex [(dien)Cu(mu-im)Cu(dien)](ClO(4))(3) and related mononuclear complexes [Cu(dien)(H(2)O)](ClO(4))(2), [Cu(dien)(Him)](ClO(4))(2) were synthesized with diethylenetriamine (dien) as capping ligand. The crystal structure of mononuclear [Cu(dien)(Him)](ClO(4))(2) and binuclear complex [(dien)Cu(mu-im)Cu(dien)](ClO(4))(3) have been determined by single crystal X-ray diffraction methods. The mononuclear complex [Cu(dien)(Him)](ClO(4))(2) crystallizes in the orthorhombic, Pca2(1) with a = 9.3420(9) A, b = 12.3750(9) A, c = 14.0830(9) A, beta = 90.000(7)(o) and Z = 4 and binuclear complex [(dien)Cu(mu-im)Cu(dien)](ClO(4))(3) crystallizes in the monoclinic space group P2(1)/a, with a = 15.017(7) A, b = 11.938(6) A, c = 15.386(6) A, beta = 110.30(4)(o) and Z = 4. The molecular structures show that copper(II) ions in an asymmetrically elongated octahedral coordination (type 4 + 1 + 1) and in binuclear complex Cu(1) atom has a asymmetrically elongated octahedral coordination (type type 4 + 1 + 1) and Cu(2) atom exhibits a square base pyramidal coordination (type 4 + 1). The bridging ligand (imidazolate ion, im) lies nearly on a straight line between two Cu(2+), which are separated by 5.812 A, slightly shorter than the value in copper-copper superoxide dismutase (Cu(2)-Cu(2)SOD). Magnetic measurements and electron spin resonance (ESR) spectroscopy of the binuclear complex have shown an antiferromagnetic exchange interaction. From pH-dependent cyclic voltametry (CV) and electronic spectroscopic studies the complex has been found to be stable over a wide pH range (7.75-12.50).


Assuntos
Cobre/química , Modelos Químicos , Compostos Organometálicos/química , Superóxido Dismutase/química , Absorção , Antibacterianos/farmacologia , Carbono/química , Cristalografia por Raios X , Eletroquímica , Eletrodos , Espectroscopia de Ressonância de Spin Eletrônica , Vidro , Concentração de Íons de Hidrogênio , Magnetismo , Conformação Molecular , Estrutura Molecular , Compostos Organometálicos/síntese química , Compostos Organometálicos/farmacologia , Soluções , Superóxido Dismutase/metabolismo
13.
J Inorg Biochem ; 98(2): 231-7, 2004 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-14729303

RESUMO

X-band electron spin resonance (ESR) and electronic spectra of oxalatobridged heterodinuclear Cu-Ni and Cu-Zn complexes, viz., [(PMDT)Cu-Ox-Ni(PMDT)](BPh(4))(2).2CH(3)CN and [(PMDT)Cu-Ox-Zn(PMDT)](BPh(4))(2).2CH(3)CN, where PMDT=pentamethyldiethylenetriamine, Ox=oxalate ion have been described. Complex [(PMDT)Cu-Ox-Ni(PMDT)](BPh(4))(2).2CH(3)CN has been structurally characterized. This complex crystallizes in the monoclinic space group, C(2) (No. 5) with the unit parameters a=20.445(4) A, b=14.884(3) A, c=23.174(5) A, alpha=90 degrees, beta=102.693(4) degrees, gamma=90 degrees, V=6880(2) A(3) and Z=4. The structure refined to R=0.0354 and R(w)=0.0853 for 21,109 reflections with I>2 sigma(I) using 765 parameters, shows the presence of a MN(3)O(2) chromophore in a distorted trigonal-bipyramidal (TBP) heterometallic complex with oxalate dianion. Taking with an equatorial Cu-O=2.137(8) A and an axial Cu-O=1.961(6) A coordination site at Cu(II) ion and equatorial Ni-O=2.178(7) A and axial Ni-O=1.994 (9) A coordination site at Ni(II) ion. The Cu-Ni distance is 5.3532(9) A and Cu-C(2)O(4)-Ni unit is planar. The [(PMDT)Cu-Ox-Ni(PMDT)](2+) shows the ESR spectrum of the antiferromagnetic spin exchange with each dinuclear delocalization of the unpaired electron over the unit and spin-doublet ground state which demonstrates the Cu-Ox-Ni core. Antimicrobial and superoxide dismutase (SOD) activities of these complexes have also been measured.


Assuntos
Antibacterianos/química , Compostos Organometálicos/química , Superóxido Dismutase/metabolismo , Animais , Antibacterianos/farmacologia , Bactérias/efeitos dos fármacos , Cobre/química , Cobre/metabolismo , Cristalografia por Raios X , Espectroscopia de Ressonância de Spin Eletrônica , Metais Pesados/química , Metais Pesados/metabolismo , Níquel/química , Níquel/metabolismo , Compostos Organometálicos/metabolismo , Compostos Organometálicos/farmacologia , Oxalatos/química , Oxalatos/metabolismo , Análise Espectral , Relação Estrutura-Atividade , Zinco/química , Zinco/metabolismo
14.
Spectrochim Acta A Mol Biomol Spectrosc ; 59(13): 3111-22, 2003 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-14583286

RESUMO

X-band e.s.r. and optical absorption spectra of the imidazolate bridged heterobimetallic complexes [(tren)Cu-E-Im-Zn-(tren)](ClO(4))(3) and [(tren)Cu-E-Im-Ni-(tren)](ClO(4))(3), where trentris(2-aminoethyl)amine, E-Im=2-ethylimidazolate ion and the related mononuclear complexes [Cu(tren)](ClO(4))(2) and [(tren)Cu-E-ImH)](ClO(4))(2) have been described. Biological activities (superoxide dismutase and antimicrobial) have also been measured and compared with reported complexes.


Assuntos
Anti-Infecciosos/química , Imidazóis/análise , Compostos Organometálicos/análise , Superóxido Dismutase , Anti-Infecciosos/farmacologia , Cobre , Espectroscopia de Ressonância de Spin Eletrônica/métodos , Enterococcus faecalis/efeitos dos fármacos , Escherichia coli/efeitos dos fármacos , Indicadores e Reagentes , Ligantes , Testes de Sensibilidade Microbiana , Modelos Moleculares , Níquel , Espectrofotometria , Zinco
17.
J Biol Chem ; 263(11): 5049-55, 1988 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-2965697

RESUMO

In the hydrolysis of MgATP by acto heavy meromyosin (HMM) there are two enzymatic pathways that differ in the properties of their intermediate oxygen exchange; one of these is designated the low exchange pathway (P1); the other is designated the high exchange pathway (P2). A plot of the P1 flux versus the actin concentration gives a sigmoid curve, whereas the corresponding curve for the P2 flux rises in an approximately hyperbolic manner. At low concentrations of actin, where the sigmoid curve of the P1 flux is in a lag phase, the major flux is along P2; but at higher concentrations of actin, as the P1 curve rises sharply, the flux along P1 comes to predominate. Even at the highest levels of actin, at saturating levels for both pathways, the kinetics of exchange along P1 and P2 are significantly different. In addition to these differences in the actin dependence, the flux of P1 relative to P2 is markedly inhibited by KCl. Therefore, which of the two pathways dominates during the hydrolysis of MgATP by HMM is strongly dependent on experimental conditions. The findings suggest that P1 involves the interaction of HMM with two actin units whereas P2 involves the interaction of HMM with one actin unit. The results are discussed in relation to a kinetic scheme based on this proposal.


Assuntos
Actinas/metabolismo , Subfragmentos de Miosina/metabolismo , Oxigênio/metabolismo , Adenosina Trifosfatases/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Quimotripsina/metabolismo , Cloreto de Potássio/metabolismo , Coelhos , Tripsina/metabolismo
18.
J Biol Chem ; 261(26): 12141-6, 1986 Sep 15.
Artigo em Inglês | MEDLINE | ID: mdl-3488992

RESUMO

At an intermediate stage in the hydrolysis of MgATP by actomyosin there is an exchange of oxygen between water and the terminal phosphoryl group of MgATP, tightly bound to the myosin active site. This intermediate oxygen exchange results from the reversible hydrolysis of the bound MgATP. The rate of the exchange cycle (hydrolysis and the reverse) is assumed to be determined by the rate of reverse hydrolysis; and the average time available for exchange is determined by the post-exchange reaction that immediately follows the cycle. Past analytical studies of the exchange, using actomyosin mixtures and myofibrils at room temperature, have revealed two pathways for hydrolysis, operating at a comparable flux but differing greatly in the extent of exchange they support. It is shown here that these pathways also appear over a range of temperatures from 5 to 30 degrees C and that temperature had little effect on their relative fluxes. At each temperature, the flux ratio (%) for the low exchange pathway: high exchange pathway was near 50:50 for actomyosin mixtures and 60:40 for myofibrils. Apparently, the rate-limiting steps that determine the fluxes of the two pathways have a similar temperature dependence. However, the analysis indicates that one or both of the steps that determine the extent of exchange (reverse-hydrolysis and/or the post-exchange reaction) shows a different temperature dependence for the two pathways. We interpret this to reflect a difference in the temperature dependence of the post-exchange reaction, which we propose is exceedingly fast and independent of actin concentration along the low exchange route, but slow and dependent on the actin concentration along the high exchange route. Thus at all temperatures over a broad range of actin concentration there are two pathways of comparable flux that differ primarily in the time available for exchange.


Assuntos
Actomiosina/metabolismo , Miofibrilas/metabolismo , Oxigênio/metabolismo , Temperatura , Actinas/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Modelos Químicos , Coelhos
19.
J Biol Chem ; 259(9): 5423-9, 1984 May 10.
Artigo em Inglês | MEDLINE | ID: mdl-6609157

RESUMO

Recent studies of oxygen exchange have shown that there are two normal pathways for the hydrolysis of MgATP by myosin in the presence of actin, each producing Pi at the same rate. These two apparent pathways for actin-activated hydrolysis differ greatly in the extent of oxygen exchange they support. This is revealed by an analysis of the distribution of [18O]Pi species produced by the hydrolysis of [gamma-18O]ATP. We have extended these studies to certain abnormal substrates, using Mn2+ in place of Mg2+, and dATP or ITP in place of ATP. The results, together with past findings, lead to the proposal that the two heads of myosin are functionally different. One of these (Head 1) is able to reversibly cleave bound MgATP and thereby support oxygen exchange while it is free of actin; the other (Head 2) cannot cleave bound MgATP at its active site while free of actin. However, in the presence of actin, both Head 1 and Head 2 cleave bound MgATP, support some oxygen exchange, and produce Pi at the same rapid actin-activated rate. Apparently, MgATP is positioned differently on the two heads when they are free of actin, with Mg2+ and the 6-amino group of ATP playing an important role in the orientation. This proposed difference between the heads could serve to make Head 1 react first with the actin filament, followed by Head 2. Thus, in muscle, the two heads on a myosin cross-bridge would interact with an actin filament and exert their pull in a fixed sequence.


Assuntos
Trifosfato de Adenosina/metabolismo , Miosinas/metabolismo , Actinas/metabolismo , Animais , Cinética , Magnésio/farmacologia , Manganês/farmacologia , Músculos/metabolismo , Subfragmentos de Miosina , Isótopos de Oxigênio , Fragmentos de Peptídeos/metabolismo , Coelhos , Especificidade por Substrato
20.
Biochemistry ; 22(20): 4822-30, 1983 Sep 27.
Artigo em Inglês | MEDLINE | ID: mdl-6354267

RESUMO

At an intermediate stage in the hydrolysis of magnesium adenosine 5'-phosphate (MgATP) by myosin or actomyosin, there is an exchange of oxygen between water and the P gamma group of enzyme-bound nucleotide. Starting with [P gamma-18O]ATP as substrate, the exchange is revealed in the [18O]Pi species that are ultimately released as product into the reaction medium. An analysis of the distribution of these labeled Pi species, which contain 3, 2, 1, or none of the 18O atoms originally on the P gamma of ATP, is used to probe intermediate stages of the hydrolytic mechanism. In recent years, studies of this kind by several groups have shown that more than one pathway of hydrolysis operates. The work reported here demonstrates that two of these pathways are spurious; one is a "nonexchanging MgATPase" that is present in fresh myosin preparations; the other is an induced slow exchange that develops in myosin during storage (-20 degrees C) and subsequent aging (4 degrees C). However, after correction for these artifacts, two normal pathways for actomyosin hydrolysis remain. These normal pathways differ in the mode of interaction between actin and myosin in the course of hydrolysis; one is the Lymn-Taylor pathway where oxygen exchange occurs at a stage when actin and myosin are dissociated; the other is a pathway in which actin and myosin are associated during oxygen exchange. Each of these two pathways contributes an equal amount of Pi to the product pool. Thus, on average, each myosin head uses each of these pathways half the time. The findings suggest, e.g., that during contraction, myosin can dissociate from the actin filament only during every other cycle of MgATP hydrolysis or that only half the heads, at any one time, can exchange oxygen while free of the actin filament.


Assuntos
Actomiosina/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Hidrólise , Cinética , Músculos/metabolismo , Subfragmentos de Miosina/metabolismo , Miosinas/metabolismo , Isótopos de Oxigênio , Fragmentos de Peptídeos/metabolismo , Coelhos , Ratos
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