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  1 / 2953 MEDLINE  
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Alves, José Donizeti
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[PMID]:27979176
[Au] Autor:Livramento KGD; Borém FM; José AC; Santos AV; Livramento DED; Alves JD; Paiva LV
[Ad] Endereço:Federal University of Lavras, CEP 37200-000 Lavras, MG, Brazil. Electronic address: kalynkagabriella@yahoo.com.br.
[Ti] Título:Proteomic analysis of coffee grains exposed to different drying process.
[So] Source:Food Chem;221:1874-1882, 2017 Apr 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many biochemical events occur inside grains during post-harvest processes. Several methods have been developed to relate the chemical composition of the coffee grain to the beverage quality, including identification of possible molecular markers for flavor characterizing. This study was aimed at evaluating the changes in the proteomic profile of pulped and natural C. arabica grains dried in a yard or dryer at 60°C. It was observed that fruits dried in a dryer at 60°C showed an altered proteomic profile, with a reduction in the most abundant proteins compared to those yard-dried grains. Among the identified proteins, those involved in the metabolism of sugars and stress response were highlighted. Results have shown that post-harvest processes that impact coffee quality are related to changes in protein abundance, indicating that proteomic analysis may be effective in the identification of biochemical changes in coffee grains subjected to different post-harvest processes.
[Mh] Termos MeSH primário: Coffea/química
Café/química
Dessecação
Manipulação de Alimentos
Proteômica
[Mh] Termos MeSH secundário: beta-Globulinas/análise
Gliceraldeído-3-Fosfato Desidrogenases/análise
Proteínas de Choque Térmico/análise
Proteínas de Plantas/análise
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Espectrometria de Massas em Tandem
UTP-Glucose-1-Fosfato Uridililtransferase/análise
alfa-Galactosidase/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Coffee); 0 (Heat-Shock Proteins); 0 (Plant Proteins); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 3.2.1.22 (alpha-Galactosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


  2 / 2953 MEDLINE  
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[PMID]:27417394
[Au] Autor:Helmich F; van Dongen JL; Kuijper PH; Scharnhorst V; Brunsveld L; Broeren MA
[Ad] Endereço:Laboratory of Chemical Biology, Department of Biomedical Engineering, Institute of Complex Molecular Systems, Eindhoven University of Technology, Expert Center Clinical Chemistry Eindhoven, The Netherlands; Laboratory for Clinical Chemistry and Hematology, Máxima Medisch Centrum, Veldhoven, Expert C
[Ti] Título:Rapid phenotype hemoglobin screening by high-resolution mass spectrometry on intact proteins.
[So] Source:Clin Chim Acta;460:220-6, 2016 Sep 01.
[Is] ISSN:1873-3492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Given the excellent performance of modern mass spectrometers, their clinical application for the analysis of macromolecules is a growing field of interest. This principle is explored by hemoglobin analysis, which is a representative example by its molecular weight and clinical relevance in e.g. screening programs for thalassemia and hemoglobin variants. Considering its abundance and cellular containment, pre-analysis is significantly reduced allowing for essential rapid acquisitions. METHODS: By parallel analysis of routine diagnostics for hemoglobin variants and thalassemia, we acquired samples of adults who were consented for hemoglobinopathy screening in our clinical laboratory. The pre-analytical process comprised of red cell lysis only; without further digestion and purification steps, the samples were directly injected in an electrospray ionization quadrupole time-of-flight setup and the intact proteins were analyzed by flow injection analysis. After optimization of process parameters, the deconvoluted mass spectra revealed the presence of α- and ß-globulins. The reference ranges for the average mass of both globulins and their intensity ratio (α/ß-ratio) were deduced from a disease-free subgroup and patients with a hemoglobinopathy were compared. RESULTS: The α/ß-ratio is a poor marker for thalassemia patients, yet deviant α/ß-ratios are found for patients with a hemoglobin variant. Mass deviations down to 1Da can be resolved; even if the patient suffers from a heterozygotic disorder, the average mass is found outside the established reference interval. CONCLUSIONS: Although subjects with mild thalassemia were not detected, all patients with a hemoglobin variant were resolved by top-down mass spectrometry using the average globulin mass and the α/ß-ratio as screening parameters.
[Mh] Termos MeSH primário: Hemoglobinopatias/diagnóstico
Hemoglobinas Anormais/análise
Espectrometria de Massas/métodos
[Mh] Termos MeSH secundário: Adulto
alfa-Globulinas/análise
beta-Globulinas/análise
Seres Humanos
Programas de Rastreamento
Valores de Referência
Espectrometria de Massas por Ionização por Electrospray/métodos
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alpha-Globulins); 0 (Beta-Globulins); 0 (Hemoglobins, Abnormal)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170202
[Lr] Data última revisão:
170202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160716
[St] Status:MEDLINE


  3 / 2953 MEDLINE  
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[PMID]:27325303
[Au] Autor:Musiol K; Sobol-Milejska G; Nowotka L; Torba K; Kniazewska M; Wos H
[Ad] Endereço:Department of Pediatric Oncology, Hematology and Chemotherapy, Upper Silesia Children's Care Health Centre, Medical University of Silesia, 40-752, Katowice, 16 Medykow Str., Poland. katkamusiol@gmail.com.
[Ti] Título:Renal function in children treated for central nervous system malignancies.
[So] Source:Childs Nerv Syst;32(8):1431-40, 2016 Aug.
[Is] ISSN:1433-0350
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:AIM: The aim of the study was to evaluate renal function and to assess the usefulness of the following nephrotoxicity markers: cystatin C (CYS C), beta-2 microglobulin (B2MG) and neutrophil gelatinase-associated lipocalin (NGAL) in 38 (18 girls, 20 boys) children previously treated for central nervous system malignancy. MATERIAL: Median age at evaluation was 13.7 years (range 2.1-22 years). The mean follow-up time after the completion of chemotherapy was 3.2 years (range 0.16-6.5 years). RESULTS: Subclinical chronic kidney disease (estimated glomerular filtration rate: eGFR 90-60 ml/min/1.73 m(2)) was found in 22 patients (58 %), while renal insufficiency (eGFR 30-60 ml/min/1.73 m(2)) was found in six children (16 %). It has been demonstrated statistically significant negative correlation between the eGFR and cystatin C concentration (p < 0.0001) and eGFR and beta-2 microglobulin concentration (p < 0.02). Conversely, there was no correlation between eGFR and NGAL. Thirteen children (34 %) developed drug-induced tubulopathy: decreased tubular reabsorption of phosphate (TRP) and renal tubular threshold for phosphate (Tmp/GFR). CONCLUSION: Children treated for CNS tumours often develop drug-induced chronic renal disease, involving the glomeruli and/or renal tubules. Cystatin C and beta-2 microglobulin seemed to be good markers for chronic kidney damage in these patients, which is probably not true for NGAL.
[Mh] Termos MeSH primário: Antineoplásicos/efeitos adversos
Nefropatias/induzido quimicamente
Nefropatias/diagnóstico
[Mh] Termos MeSH secundário: Adolescente
beta-Globulinas/metabolismo
Neoplasias do Sistema Nervoso Central/tratamento farmacológico
Criança
Pré-Escolar
Cistatina C/metabolismo
Feminino
Seguimentos
Taxa de Filtração Glomerular
Seres Humanos
Nefropatias/metabolismo
Lipocalina-2/metabolismo
Masculino
Estatísticas não Paramétricas
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Beta-Globulins); 0 (Cystatin C); 0 (Lipocalin-2)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE
[do] DOI:10.1007/s00381-016-3130-2


  4 / 2953 MEDLINE  
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[PMID]:26596012
[Au] Autor:Yuan H; Song Y; Zhang D
[Ti] Título:[Clinical observation of the γ-globulin levels when Benign paroxysmal positional vertigo is attacking].
[So] Source:Lin Chung Er Bi Yan Hou Tou Jing Wai Ke Za Zhi;29(10):931-3, 2015 May.
[Is] ISSN:1001-1781
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To observe the characteristics of serum protein in patients with benign paroxysmal positional vertigo (BPPV) during the symptomatic period. METHOD: Fifty-five patients with BPPV and 58 control subjects were enrolled in the study. All the patients underwent the Dixe-Hallpike and Roll maneuver to confirm the type of BPPV. The average time of onset was (1.0 ± 0.8)days in the group of BPPV. The clinical features and the laboratory tests of serum protein electrophoresis, blood counts, and liver and kidney function were performed in both groups. RESULT: The levels of serum albumin (Alb), α1 globulin, α2 globulin and ß globulin of BPPV group did not differ statistically in the two groups (P > 0.05); The γ-globulin levels were significantly higher in patients with BPPV than in controls (P < 0.05). CONCLUSION: The γ-globulin levels are increased when BPPV is attacking.
[Mh] Termos MeSH primário: Vertigem Posicional Paroxística Benigna/sangue
Vertigem Posicional Paroxística Benigna/diagnóstico
gama-Globulinas/análise
[Mh] Termos MeSH secundário: alfa-Globulinas/análise
beta-Globulinas/análise
Estudos de Casos e Controles
Seres Humanos
Albumina Sérica/análise
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alpha-Globulins); 0 (Beta-Globulins); 0 (Serum Albumin); 0 (gamma-Globulins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151124
[Lr] Data última revisão:
151124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE


  5 / 2953 MEDLINE  
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[PMID]:25576236
[Au] Autor:Andrich F; Richardson M; Naumann GB; Cordeiro MN; Santos AV; Santos DM; Oliveira JS; de Lima ME; Figueiredo SG
[Ad] Endereço:Departamento de Ciências Fisiológicas, Centro de Ciências da Saúde, Universidade Federal do Espírito Santo, Avenida Marechal Campos, 1468, Maruípe, Vitória, ES 29043-900, Brazil; Departamento de Fisiologia e Biofísica, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Avenida A
[Ti] Título:Identification of C-type isolectins in the venom of the scorpionfish Scorpaena plumieri.
[So] Source:Toxicon;95:67-71, 2015 Mar.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chemical analyses of the hemagglutinating fraction from Scorpaena plumieri venom revealed that it contains five components (Sp-CL 1-5) with similar chromatographic elution profiles (35-38% of acetonitrile), molecular masses (16,800-17,000 Da) and N-terminal sequences, suggesting that they are isoforms of the same protein. The amino acid sequence of Sp-CL4 was determined and shown to have homology with fish C-type lectins. These data demonstrate for the first time the presence of C-type isolectins in a scorpionfish venom.
[Mh] Termos MeSH primário: Venenos de Peixe/química
Lectinas/isolamento & purificação
Perciformes
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
beta-Globulinas/química
beta-Globulinas/isolamento & purificação
Venenos de Peixe/isolamento & purificação
Lectinas/química
Lectinas Tipo C/química
Lectinas Tipo C/isolamento & purificação
Dados de Sequência Molecular
Peso Molecular
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Fish Venoms); 0 (Lectins); 0 (Lectins, C-Type); 0 (hemagglutination enhancing factor)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150202
[Lr] Data última revisão:
150202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150111
[St] Status:MEDLINE


  6 / 2953 MEDLINE  
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[PMID]:25308024
[Au] Autor:Parab S; Sakhare S; Sengupta C; Velumani A
[Ti] Título:Diagnosis of a rare double heterozygous Hb D Punjab/Hb Q India hemoglobinopathy using Sebia capillary zone electrophoresis.
[So] Source:Indian J Pathol Microbiol;57(4):626-8, 2014 Oct-Dec.
[Is] ISSN:0974-5130
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:In India, hemoglobinopathies constitute a major genetic disorder and hemoglobin variants such as Hb S, Hb D Punjab, and Hb E are the most common ones. Other variants include Hb Q India, Hb Lepore, Hb J Meerut, Hb D Iran, etc. These variants show heterozygous state along with beta thalassemia. However, compound heterozygosities among these variants are very rare. Ethylenediaminetetraacetic acid whole blood sample received for routine thalassemia screening was subjected to alkaline electrophoresis using automated capillary zone electrophoresis. Suspecting the presence of rare variants, further analysis was carried out using Bio-Rad D10 and Tosoh G8 high-performance liquid chromatography (HPLC) systems. Capillary zone electrophoretograms showed the presence of peaks in zone Hb A, Hb D, a fused peak in Hb A2, and a small peak in Z1 zone. Bio-Rad and Tosoh chromatograms also indicated the presence of four peaks which are identified as Hb A, Hb D Punjab, Hb Q India, and hybrid of Hb D Punjab/Hb Q India. A peak in Hb D zone of capillary was due to co-migration of Hb D Punjab and Hb Q India variants. Small peak in Z1 zone indicated the presence of alpha chain variant Hb Q India. The findings were further confirmed by HPLC results and molecular genetic studies. The present study reports for the 1st time a rare hemoglobinopathy of double heterozygosity for Hb D Punjab, Hb Q India on Capillarys 2 Flex Piercing analyzer and is forth reported case for this rare hemoglobinopathy.
[Mh] Termos MeSH primário: Hemoglobinopatias/diagnóstico
Hemoglobinopatias/genética
Hemoglobinas Anormais/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
beta-Globulinas/genética
Eletroforese Capilar
Seres Humanos
Índia
Reação em Cadeia da Polimerase
alfa-Globinas/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Hemoglobins, Abnormal); 0 (alpha-Globins); 39340-63-1 (hemoglobin Q India); 9034-60-0 (hemoglobin D Punjab)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:141013
[Lr] Data última revisão:
141013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141014
[St] Status:MEDLINE
[do] DOI:10.4103/0377-4929.142709


  7 / 2953 MEDLINE  
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[PMID]:25267517
[Au] Autor:Bugier S; Dedome E; Fontan E; Ceppa F; Delacour H
[Ad] Endereço:Department of Biology, French Military Teaching Hospital, Saint Mandé, France.
[Ti] Título:It's just an illusion.
[So] Source:Clin Chem;60(10):1351-2, 2014 Oct.
[Is] ISSN:1530-8561
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: beta-Globulinas/análise
Eletroforese Capilar/métodos
Eletroforese Capilar/normas
[Mh] Termos MeSH secundário: Meios de Contraste/administração & dosagem
Meios de Contraste/farmacocinética
Reações Falso-Positivas
Seres Humanos
Iopamidol/administração & dosagem
Iopamidol/análogos & derivados
Iopamidol/farmacocinética
Masculino
Meia-Idade
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Contrast Media); 17E17JBP8L (iomeprol); JR13W81H44 (Iopamidol)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:140930
[Lr] Data última revisão:
140930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141001
[St] Status:MEDLINE
[do] DOI:10.1373/clinchem.2013.220921


  8 / 2953 MEDLINE  
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[PMID]:23838325
[Au] Autor:Zhang A; Yu H; He Y; Shen Y; Pan N; Liu J; Fu B; Miao F; Zhang J
[Ad] Endereço:Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Department of Microbiology and Immunology, Medical School, Southeast University, Nanjing, Jiangsu 210009, China.
[Ti] Título:The spatio-temporal expression of MHC class I molecules during human hippocampal formation development.
[So] Source:Brain Res;1529:26-38, 2013 Sep 05.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the immune system, the major histocompatibility complex (MHC) class I molecules mediate both the innate and adaptive immune responses in vertebrates. There has been a dogma that the central nervous system (CNS) is immune privileged and healthy neurons do not express MHC class I molecules. However, recent studies have indicated that the expression and non-immunobiologic roles of MHC class I in mammalian CNS. But data referring to humans are scarce. In this study we report the expression and cellular localization of MHC class I in the human fetal, early postnatal and adult hippocampal formation. The expression of MHC class I was very low in the hippocampus at 20 (gestational weeks) GW and slowly increased at 27-33 GW. The gradually increased expression in the somata of some granular cells in dentate gyrus (DG) was observed at 30-33 GW. Whereas, a rapid increase in MHC class I molecules expression was found in the subiculum and it reached high levels at 31-33 GW and maintained at postnatal 55 days. No expression of MHC class I was found in hippocampal formation in adult. MHC class I heavy chain and ß2 microglobulin (ß2M) showed similar expression in some cells of the hippocampal formation at 30-33 GW. Moreover, MHC class I molecules were mainly expressed in neurons and most MHC class I-expressing neurons were glutamatergic. The temporal and spatial patterns of MHC class I expression appeared to follow gradients of pyramidal neurons maturation in the subiculum at prenatal stages and suggested that MHC class I molecules are likely to regulate neuron maturation. This article is part of a Special Issue entitled Priority to Publish.
[Mh] Termos MeSH primário: Encéfalo
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Hipocampo
Antígenos de Histocompatibilidade Classe I/metabolismo
[Mh] Termos MeSH secundário: Adulto
Autopsia
beta-Globulinas/metabolismo
Encéfalo/anatomia & histologia
Encéfalo/embriologia
Encéfalo/crescimento & desenvolvimento
Feto
Idade Gestacional
Proteína Glial Fibrilar Ácida/metabolismo
Hipocampo/embriologia
Hipocampo/crescimento & desenvolvimento
Hipocampo/metabolismo
Seres Humanos
Lactente
Proteínas do Tecido Nervoso/metabolismo
Fosfopiruvato Hidratase/metabolismo
Proteína Vesicular 1 de Transporte de Glutamato/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Glial Fibrillary Acidic Protein); 0 (Histocompatibility Antigens Class I); 0 (Nerve Tissue Proteins); 0 (SLC17A7 protein, human); 0 (Vesicular Glutamate Transport Protein 1); 56-12-2 (gamma-Aminobutyric Acid); EC 4.2.1.11 (Phosphopyruvate Hydratase)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:130819
[Lr] Data última revisão:
130819
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130711
[St] Status:MEDLINE


  9 / 2953 MEDLINE  
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[PMID]:23577895
[Au] Autor:Mayahi M; Khajeh G; Mosavari N; Parvandar Asadollahi K; Akhavizadegan MA
[Ad] Endereço:Department of Clinical Science, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
[Ti] Título:Serum protein profiles in domestic pigeons naturally infected with Mycobacterium avium subsp. avium.
[So] Source:Vet Clin Pathol;42(2):212-5, 2013 Jun.
[Is] ISSN:1939-165X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Avian tuberculosis is an important disease affecting all species of birds and is most often caused by Mycobacterium avium or Mycobacterium genavense. Blood proteins are important diagnostic constituents in gastrointestinal, hepatic, renal, and infectious diseases. OBJECTIVE: The aim of the study was to compare serum protein profiles of domestic pigeons (Columba livia var. domestica) infected with Mycobacterium avium subsp. avium (MAA), with healthy pigeons. METHODS: Serum samples were collected from 80 pigeons with clinical signs of tuberculosis, all kept in the same loft. All birds were necropsied and cultured for mycobacteriosis; positive cultures were typed for MAA by PCR reactions targeting 16S rRNA, IS901 and IS1245. The concentration of total serum proteins was determined by the biuret method and spectrophotometry. Individual protein fractions were analyzed by cellulose acetate electrophoresis and extrapolated based on total protein concentration. For statistical analysis, the infected birds were compared with healthy pigeons. RESULTS: A total of 37 pigeons with culture results positive for MAA were selected and allocated to 2 groups, a culture-positive group with macroscopic lesions of tuberculosis and another without macroscopic lesions. Six protein fractions were identified: prealbumin, albumin, alpha-1, alpha-2, and beta globulins and gamma globulins. Concentrations of total protein, beta globulins and gamma globulins were statistically significantly higher in the infected pigeons when compared with the control group. There were no significant differences between the groups of birds with or without macroscopic lesions. CONCLUSIONS: Statistically significant differences in total protein, and beta and gamma globulin concentrations in all infected pigeons suggest that serum protein electrophoresis represents a nonspecific but valuable indicator for tuberculosis in pigeons.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/metabolismo
Columbidae
Mycobacterium avium/isolamento & purificação
Tuberculose Aviária/diagnóstico
[Mh] Termos MeSH secundário: Animais
Técnicas de Tipagem Bacteriana/veterinária
beta-Globulinas/metabolismo
Eletroforese das Proteínas Sanguíneas/veterinária
DNA Bacteriano/genética
Seres Humanos
Mycobacterium avium/genética
Reação em Cadeia da Polimerase/veterinária
Tuberculose Aviária/sangue
Tuberculose Aviária/metabolismo
Tuberculose Aviária/microbiologia
gama-Globulinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Beta-Globulins); 0 (Blood Proteins); 0 (DNA, Bacterial); 0 (gamma-Globulins)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130413
[St] Status:MEDLINE
[do] DOI:10.1111/vcp.12033


  10 / 2953 MEDLINE  
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[PMID]:23571356
[Au] Autor:Adekile AD
[Ad] Endereço:Department of Pediatrics, Faculty of Medicine, Health Sciences Centre, Kuwait University, Jabriya, Kuwait. Adekile@hsc.edu.kw
[Ti] Título:What's new in the pathophysiology of sickle cell disease?
[So] Source:Med Princ Pract;22(4):311-2, 2013.
[Is] ISSN:1423-0151
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Mh] Termos MeSH primário: Anemia Falciforme/fisiopatologia
[Mh] Termos MeSH secundário: Anemia Falciforme/genética
Arginase/metabolismo
Arteriopatias Oclusivas/fisiopatologia
beta-Globulinas/genética
Endotélio Vascular/fisiopatologia
Hemólise
Seres Humanos
Inflamação/fisiopatologia
Óxido Nítrico/sangue
Trombina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Beta-Globulins); 31C4KY9ESH (Nitric Oxide); EC 3.4.21.5 (Thrombin); EC 3.5.3.1 (Arginase)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130411
[St] Status:MEDLINE
[do] DOI:10.1159/000350283



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