Search results for: Myoglobin
#33978975 2021/05/12 To Up
Efficacy and safety of the clearum dialyzer.The Clearum dialyzer, built by Medtronic, became commercially available in several European countries in 2020 but there are still no reports of in vivo data. The aim of this study was to evaluate the efficacy and risk of hypoalbuminemia of this dialyzer compared with previously evaluated hemodialysis (HD), expanded hemodialysis (HDx) and postdilution hemodiafiltration (HDF) treatments. A prospective study was carried out in 15 patients. Each patient underwent seven dialysis sessions: FX80 Cordiax in HD, Clearum HS17 in HD, Philter 17-SD in HDx, Theranova 400 in HDx, Philter 17-G in postdilution HDF, Clearum HS17 in postdilution HDF and FX80 Cordiax in postdilution HDF. The reduction ratios (RR) of urea, creatinine, ß -microglobulin, myoglobin, prolactin, α -microglobulin, α -acid glycoprotein, and albumin were compared intraindividually. Dialysate albumin loss was also measured. Comparison of dialysis techniques revealed no differences between small molecules, but HDx and HDF were significantly higher than HD with medium and large molecular weights. The Clearum dialyzer in HDF obtained similar results to FX80 Cordiax in HDF, was slightly superior to Philter 17-G in HDF and was statistically superior to both dialyzers in HDx. Albumin losses with the Clearum dialyzer were among the lowest, both in HD and HDF treatments. The highest global removal score values were obtained with the helixone and Clearum dialyzers in HDF, with similar results both in HD and HDF. In addition, the global removal score values with HDx treatments were statistically significantly higher than those with HD. The new Clearum dialyzer has excellent behavior and tolerance in HD and HDF. Its adequate permeability has been proven with its maximal performance in HDF, which could represent an upgrade versus its predecessor polyphenylene dialyzers.
Francisco Maduell, José Jesús Broseta, Diana Rodríguez-Espinosa, Evelyn Hermida-Lama, Elena Cuadrado-Payán, Lida María Rodas, Miquel Gómez, Marta Arias-Guillén, Néstor Fontseré, Manel Vera, Nayra Rico125 mg500 Units2.5 mg1000 tests100ug200ul10 mg100ul100 mg 100ul
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Exercise Induced Myoglobinuria is Determined by Haptoglobin Polymorphism.In professional soccer players (n = 27), confounders of quantitative myoglobinuria following physical training were assessed in order to improve interpretation of post-exercise myoglobinuria.
Thomas M Maenhout, Tijl Vermassen, Lode Dalewyn, Marc L De Buyzere, Joris R Delanghe
2423 related Products with: Exercise Induced Myoglobinuria is Determined by Haptoglobin Polymorphism.50 ul100 ul100 ul100 ul50 ul100 ul100ug Lyophilized100 ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized
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Effect of alfalfa (Medicago sativa L.) saponins on meat color and myoglobin reduction status in the longissimus thoracis muscle of growing lambs.The effect of alfalfa saponins (AS) supplementation on the meat quality especially the color for growing lamb was investigated. Fifty Hu male lambs with body weights (BW, 19.21 ± 0.45 kg) were divided into five groups and supplemented AS with 0, 500, 1,000, 2,000, and 4,000 mg/kg of dietary dry matter intake. After 90 days, all lambs were slaughtered. The longissimus thoracis muscle in lamb displayed significant changes in the content of intramuscular fat, especially n-3 polyunsaturated fatty acids, and drip loss within AS treatment (p < .05) between control and treatments groups. Redness (a*) significantly improved in both 0-day and 7-day storage with the AS supplementation coupled with the percentage of met-myoglobin reduction (p < .05). The redness (a*) change may result from improved met-myoglobin reducing activity, antioxidant enzymes, lactate dehydrogenase, and succinate dehydrogenase (p < .05) by AS supplementation in muscle. These enzymes may help to protect mitochondria function and reduce met-myoglobin, which bring a bright and red meat color.
Ce Liu, Chen-Chen Xu, Yang-Hua Qu, Ping-Ting Guo, Yong Ma, Bo Wang, Hao Zhang, Hai-Ling Luo
2548 related Products with: Effect of alfalfa (Medicago sativa L.) saponins on meat color and myoglobin reduction status in the longissimus thoracis muscle of growing lambs.1 5 G
#33969705 2021/05/10 To Up
On the potential role of globins in brown adipose tissue: a novel conceptual model and studies in myoglobin knockout mice.Myoglobin (Mb) regulates O bioavailability in muscle and heart as partial pressure of O (pO) drops with increased tissue workload. Globin proteins also modulate cellular NO pools, "scavenging" NO at higher pO and converting NO to NO as pO falls. Myoglobin binding of fatty acids may also signal a role in fat metabolism. Interestingly, Mb is expressed in brown adipose tissue (BAT), but its function is unknown. Herein, we present a new conceptual model that proposes links between BAT thermogenic activation, concurrently reduced pO, and NO pools regulated by deoxy/oxy-globin toggling and xanthine oxidoreductase (XOR). We describe the effect of Mb knockout (Mb) on BAT phenotype (lipid droplets, mitochondrial markers uncoupling protein 1 [UCP1] and cytochrome C oxidase 4 [Cox4], transcriptomics) in male and female mice fed a high fat diet (HFD, 45% of energy, ~13 wk), and examine Mb expression during brown adipocyte differentiation. Interscapular BAT weights did not differ by genotype, but there was a higher prevalence of mid-large sized droplets in Mb. COX4 protein expression was significantly reduced in Mb BAT, and a suite of metabolic/NO/stress/hypoxia transcripts were lower. All of these Mb-associated differences were most apparent in females. The new conceptual model, and results derived from Mb mice, suggest a role for Mb in BAT metabolic regulation, in part through sexually dimorphic systems and NO signaling. This possibility requires further validation in light of significant mouse-to-mouse variability of BAT Mb mRNA and protein abundances in wildtype mice and lower expression relative to muscle and heart.
Michael L Blackburn, Umesh D Wankhade, Kikumi D Ono-Moore, Sree V Chintapalli, Renee Fox, Jennifer M Rutkowsky, Brandon J Willis, Todd Tolentino, K C Kent Lloyd, Sean H Adams
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#33969704 2021/05/10 To Up
Metabolic physiology and skeletal muscle phenotypes in male and female myoglobin knockout mice.Myoglobin (Mb) is a regulator of O bioavailability in type I muscle and heart, at least when tissue O levels drop. Mb also plays a role in regulating cellular NO pools. Robust binding of long-chain fatty acids and long-chain acylcarnitines to Mb, and enhanced glucose metabolism in hearts of Mb knockout (KO) mice, suggests additional roles in muscle intermediary metabolism and fuel selection. To evaluate this hypothesis, we measured energy expenditure (EE), respiratory exchange ratio (RER), body weight gain and adiposity, glucose tolerance and insulin sensitivity in Mb knockout (Mb) and wildtype (WT) mice challenged with a high fat diet (HFD, 45% of calories). In males (n=10/genotype) and females (n=9/genotype) aged 5-6, 11-12, and 17-18 wk, there were no genotype effects on RER, EE, or food intake. RER and EE during cold (10˚C, 72 h), and glucose and insulin tolerance, were not different compared to within-sex WT controls. At ~18 and ~19 wk of age, female Mb adiposity was ~42-48% higher vs. WT females (p=0.1). Transcriptomics analyses (whole gastrocnemius, soleus) revealed few consistent changes, with the notable exception of a 20% drop in soleus transferrin receptor (Tfrc) mRNA. Capillarity indices were significantly increased in Mb, specifically in Mb-rich soleus and deep gastrocnemius. The results indicate that Mb loss does not have a major impact on whole-body glucose homeostasis, EE, RER, or response to a cold challenge in mice. However, the greater adiposity in female Mb mice indicates a sex-specific effect of Mb KO on fat storage and feed efficiency.
Kikumi D Ono-Moore, I Mark Olfert, Jennifer M Rutkowsky, Sree V Chintapalli, Brandon J Willis, Michael L Blackburn, D Keith Williams, Juliana O'Reilly, Todd Tolentino, K C Kent Lloyd, Sean H Adams
2928 related Products with: Metabolic physiology and skeletal muscle phenotypes in male and female myoglobin knockout mice.500 MG100ug25 mg10 mg50 ug 50 mg100ul25 mg96T100ug
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Reduced Scattering Coefficient During Incremental Exercise Is Constant Without Being Affected by Changes in Muscle Oxygenation or Hemodynamics.Previous studies have reported that the reduced scattering coefficient (μ') in the vastus lateralis changes during ramp-incremental exercise due to blood volume changes or accumulation of metabolic by-products. We aimed to clarify the influences of deoxygenation and blood volume changes during exercise on μ' dynamics in subjects with various aerobic capacities. Twenty-three healthy young men participated in this study. All subjects performed a ramp-incremental cycling exercise until exhaustion and were divided into two groups: lower (Low: n = 12; peak pulmonary oxygen uptake per kg of fat-free mass (VO), 54.2 ± 5.3 mL/kg/min) and higher aerobic capacity group (High: n = 11; VO, 69.7 ± 5.2 mL/kg/min) by median of VO. Deoxygenated hemoglobin and myoglobin concentrations (deoxy[Hb + Mb]) and total [Hb + Mb] (total[Hb + Mb]) in the vastus lateralis were monitored during the exercise by three-wavelength (760, 800, and 830 nm) time-resolved NIRS. Similarly, μ' at each wavelength was continuously monitored. With increasing exercise intensity, deoxy[Hb + Mb] and total[Hb + Mb] significantly increased in both groups, and the average values of the peak amplitudes of deoxy[Hb + Mb] and total[Hb + Mb] during exercise showed a 106.4% increase and a 17.9% increase from the start of the exercise, respectively. Furthermore, the peak amplitude of total[Hb + Mb] was significantly greater in High. Conversely, there were no changes in μ' at any wavelength during exercise and no differences between two groups, suggesting that the great deoxygenation and blood volume changes during incremental exercise have little effect on μ' dynamics.
Tasuki Endo, Ryotaro Kime, Sayuri Fuse, Norio Murase, Yuko Kurosawa, Takafumi Hamaoka
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Near-Infrared Spectroscopy (NIRS) of Muscle HbO and MbO Desaturation During Exercise.Continuous noninvasive monitoring of muscle oxygenation has important clinical applications for muscle disorders such as compartmentation syndrome, fibromyalgia, deep vein thrombosis, malignant hyperthermia, and the assessment of training in athletic performance. NIRS has precisely such potential and has been used to detect deep venous thrombosis, evaluate athletic performance, and assess limb reperfusion and revascularization. The aim of this study was to examine the relationship between muscle hemoglobin oxygen (HbO) and myoglobin (MbO) desaturation using NIRS combined with venous blood sampling and HbO desaturation during forearm muscle exercise. Eleven normal subjects were studied, with informed consent and an IRB-approved protocol. A NIRS sensor (INVOS4100, Somanetics, Corp.) was applied on the volar aspect of the forearm. The subjects exercised their forearm by clenching and relaxing their fist while observing the oximeter and driving the reading to specified levels from 90% to 15% (minimum possible reading). Venous blood samples were withdrawn for measurement of blood gases and oxygen saturation (IL-Co-Oximeter). RSO (%) vs VO Sat showed a two-component HbO desaturation suggesting representation of venous HbO desaturation and perhaps myoglobin oxygen (MBO) desaturation. Subtraction of the linear venous HbO curve from the two-component curve suggests MbO desaturation at venous hemoglobin oxygen saturation of about 10-20%. Conclusions: The kinetics of desaturation during exercise revealed two components representing HbO and MbO deoxygenation. The data show that MbO represents approximately 40% of the NIRS signal and the balance or 60% to HbO.
Edwin M Nemoto
1605 related Products with: Near-Infrared Spectroscopy (NIRS) of Muscle HbO and MbO Desaturation During Exercise.6 mL100ug100ul 6 ml Ready-to-use 100 mg100ul1 mg1000 tests200ul1 ml0.5 ml500 MG
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Skeletal Muscle Deoxygenation and Its Relationship to Aerobic Capacity During Early and Late Stages of Aging.The aim of this study was to compare muscle O dynamics during exercise among elderly (n = 10, age: 73 ± 3 years), middle-aged (n = 9, age: 50 ± 6 years), and young (n = 10, age: 25 ± 3 years) adults. The subjects performed ramp bicycle exercise until exhaustion. Muscle O saturation (SmO) and relative changes from rest in oxygenated hemoglobin/myoglobin (∆oxy-Hb/Mb), deoxygenated hemoglobin/myoglobin (∆deoxy-Hb/Mb), and total hemoglobin concentration (∆total-Hb) were monitored continuously at the vastus lateralis muscle by near-infrared spatial resolved spectroscopy. At given absolute workloads, SmO and ∆oxy-Hb/Mb were significantly lower in elderly than the other groups, while ∆deoxy-Hb/Mb, ∆total-Hb, and pulmonary O uptake (VO) were similar among the three groups. In contrast, there were no significant differences in muscle O dynamics during submaximal exercise between middle-aged and young subjects. Muscle O dynamics may be relatively preserved in early stages of aging, although muscle deoxygenation is enhanced in late stages of aging, probably due to reduced convective O supply. Moreover, change in SmO was significantly positively correlated with peak VO in the elderly, while a significant negative relationship was observed in middle-aged and young subjects. In late stages of aging, diminished peak VO may be caused by attenuated convective O transport, while reduced peak VO can be explained by lowered muscle O extraction in early stages of aging.
Shun Takagi, Ryotaro Kime, Norio Murase, Masatsugu Niwayama, Shizuo Sakamoto, Toshihito Katsumura
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#33961840 2021/05/04 To Up
Moving beyond static snapshots: Protein dynamics and the Protein Data Bank.Proteins are the molecular machines of living systems. Their dynamics are an intrinsic part of their evolutionary selection in carrying out their biological functions. Although more difficult to observe than a static, average structure, we are beginning to observe these dynamics and form sound mechanistic connections between structure, dynamics and function. This progress is highlighted in case studies from myoglobin and adenylate kinase to the ribosome and molecular motors where these molecules are being probed with a multitude of techniques across many timescales. New approaches to time-resolved crystallography are allowing simple 'movies' to be taken of proteins in action and new methods of mapping the variations in cryo-electron microscopy are emerging to reveal a more complete description of life's machines. The results of these new methods are aided in their dissemination by continual improvements in curation and distribution by the Protein Data Bank and their partners around the world.
Mitchell D Miller, George N Phillips
1144 related Products with: Moving beyond static snapshots: Protein dynamics and the Protein Data Bank.100ul1mg100 U1021000 TESTS/0.65ml10051 Set200 1 Set50
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