• Title/Summary/Keyword: Myoglobin (Mb)

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Tests for Acute Coronary Syndrome (급성관동맥증후군 관련 검사)

  • Kim, Kyung-Dong
    • Journal of Yeungnam Medical Science
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    • v.18 no.1
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    • pp.13-29
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    • 2001
  • The enzyme activities of creatine kinase (CK), its isoenzyme MB (CK-MB) and of lactate dehydrogenase isoenzyme 1 (LD-1) have been used for years in diagnosing patients with chest pain in order to differentiate patients with acute myocardial infarction (AMI) from non-AMI patients. These methods are easy to perform as automated analyses, but they are not specific for cardiac muscle damage. During the early 90's the situation changed. First, creatine kinase ME mass (CK-MB mass) replaced the measurement of CK-MB activity. Subsequently cardiac-specific proteins, troponin T (cTnT) and troponin I (cTnI) appeared and displacing LD-1 analysis. However, troponin concentrations in blood increase only from four to six hours after onset of chest pain. Therefore a rapid marker such as myoglobin, fatty acid binding protein or glycogen phosphorylase BB could be used in early diagnosis of AMI. On the other hand, CK-MB isoforms alone may also be useful in rapid diagnosis of cardiac muscle damage. Myoglobin, CK-MB mass, cTnT and cTnI are nowadays widely used in diagnosing patients with acute chest pain. Myoglobin is not cardiac-specific and therefore requires supplementation with some other analyses such as troponins to support the myoglobin value. Troponins are very highly cardiac-specific. Only the sera of some patients with severe renal failure, which requires hemodialysis, have elevated cTnT and/or cTnI without there being any evidence of cardiac damage. The latest studies have shown that elevated troponin levels in sera of hemodialysis patients point to an increased risk of future cardiac events in a similar manner to the elevated troponin values in sera of patients with unstable angina pectoris. In addition, the bedside tests for cTnT and cTnI alone- or together with myoglobin and CK-ME mass can be used instead of quantitative analyses in the diagnosis of patients with chest pain. These rapid tests are easy to perform and they do not require expensive instrumentation. For the diagnosis of patient with chest pain, routinely myoglobin and CK-ME mass measurements should be performed whenever they are requested (24 h/day) and cTnT or cTnI on admission to the hospital and then 4-6 and 12 hours later and maintained less than 10% in imprecision.

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Structural Dynamics of Myoglobin Probed by Femtosecond Infrared Spectroscopy of the Amide Band

  • Kim, Seong-Heun;Jin, Geun-Young;Lim, Man-Ho
    • Bulletin of the Korean Chemical Society
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    • v.24 no.10
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    • pp.1470-1474
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    • 2003
  • The dynamics of the tertiary conformation of myoglobin (Mb) after photolysis of carbon monoxide was investigated at 283 K solution by probing amide I and II bands using femtosecond IR absorption spectroscopy. Time-resolved spectra in the amide region evolve with 6-12 ps time scale without noticeable subpicosecond dynamics. The spectra measured at 100 ps delay after photolysis is similar to the difference FTIR spectrum at equilibrium. Time-resolved spectra of photoexcited Mb evolve modestly and their amplitudes are less than 8% of those of photolyzed MbCO, indicating that thermal contribution to the spectral evolution in the amide region is negligible. These observations suggest that the conformational relaxation ensuing photolysis of MbCO be complex and the final deoxy protein conformation have been substantially formed by 100 ps, probably with 6- 12 ps time constant.

Direct Electrochemistry and Electrocatalysis of Myoglobin with CoMoO4 Nanorods Modified Carbon Ionic Liquid Electrode

  • Zhao, Zengying;Cao, Lili;Hu, Anhui;Zhang, Weili;Ju, Xiaomei;Zhang, Yuanyuan;Sun, Wei
    • Bulletin of the Korean Chemical Society
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    • v.34 no.2
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    • pp.475-481
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    • 2013
  • By using ionic liquid 1-hexylpyridinium hexafluorophosphate ($HPPF_6$) based carbon ionic liquid electrode (CILE) as the substrate electrode, a $CoMoO_4$ nanorods and myoglobin (Mb) composite was casted on the surface of CILE with chitosan (CTS) as the film forming material to obtain the modified electrode (CTS/$CoMoO_4$-Mb/CILE). Spectroscopic results indicated that Mb retained its native structures without any conformational changes after mixed with $CoMoO_4$ nanorods and CTS. Electrochemical behaviors of Mb on the electrode were carefully investigated by cyclic voltammetry with a pair of well-defined redox peaks from the heme Fe(III)/Fe(II) redox center of Mb appeared, which indicated that direct electron transfer between Mb and CILE was realized. Electrochemical parameters such as the electron transfer number (n), charge transfer coefficient (${\alpha}$) and electron transfer rate constant ($k_s$) were estimated by cyclic voltammetry with the results as 1.09, 0.53 and 1.16 $s^{-1}$, respectively. The Mb modified electrode showed good electrocatalytic ability toward the reduction of trichloroacetic acid in the concentration range from 0.1 to 32.0 mmol $L^{-1}$ with the detection limit as 0.036 mmol $L^{-1}$ ($3{\sigma}$), and the reduction of $H_2O_2$ in the concentration range from 0.12 to 397.0 ${\mu}mol\;L^{-1}$ with the detection limit as 0.0426 ${\mu}mol\;L^{-1}$ ($3{\sigma}$).

Conformational Dynamics of Heme Pocket in Myoglobin and Hemoglobin

  • Kim, Seong-Heun;Heo, Jeong-Hee;Lim, Man-Ho
    • Bulletin of the Korean Chemical Society
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    • v.26 no.1
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    • pp.151-156
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    • 2005
  • The conformational dynamics of heme pocket, a small vacant site near the binding site of heme proteins -myoglobin (Mb) and hemoglobin (Hb), was investigated after photolysis of carbon monoxide from MbCO and HbCO in D$_2$O solution at 283 K by probing time-resolved vibrational spectra of photolyzed CO. Two absorption bands, arising from CO in the heme pocket, evolve nonexponentially in time. The band at higher energy side blue shifts and broadens with time and the one at lower energy side narrows significantly with a negligible shift. These spectral evolutions are induced by protein conformational changes following photolysis that modify structure and electric field of heme pocket, and ligand dynamics in it. The conformational changes affecting the spectrum of photolyzed CO in heme pocket likely modulates ligand-binding activity.

Cardiac Damage Biomarkers Following a Triathlon in Elite and Non-elite Triathletes

  • Park, Chan-Ho;Kim, Kwi-Baek;Han, Jin;Ji, Jin-Goo;Kwak, Yi-Sub
    • The Korean Journal of Physiology and Pharmacology
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    • v.18 no.5
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    • pp.419-423
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    • 2014
  • The purpose of the present study was to investigate cardiac damage biomarkers after a triathlon race in elite and non-elite athlete groups. Fifteen healthy men participated in the study. Based on performance, they were divided into elite athlete group (EG: n=7) and non-elite athlete group (NEG: n=8). Participants' blood samples were obtained during four periods: before, immediately, 2 hours and 7 days after finishing the race. creatine kinase (CK), creatine kinase-myoglobin (CK-MB), myoglobin, and lactate dehydrogenase (LDH) were significantly increased in both groups immediately after, and 2 hours after finishing the race (p<.05). CK, CK-MB, and myoglobin were completely recovered after 7 days (p<.05). Hematocrit (Hct) was significantly decreased in both groups (p<.05) 7 days after the race. LDH was significantly decreased in the EG (p<.05) only 7 days after the race. Homoglobin (Hb) was significantly decreased in the NEG (p<.05) only 2 hours after the race. Although cardiac troponin T (cTnT) was significantly increased in the EG but not in the NEG 2hours after the race (p<.05), there was no group-by-time interaction. cTnT was completely recovered in both groups 7 days after the race. In conclusion, cardiac damage occurs during a triathlon race and, is greater in elite than in non-elite. However, all cardiac damage markers return to normal range within 1 week.

셀레늄 급여원에 따른 쇠고기의 육색 안정성 비교 연구

  • Park, Beom-Yeong;Seong, Pil-Nam;Kim, Dong-Hun;Ha, Gyeong-Hui;Lee, Seong-Hun;Lee, Jong-Mun;An, Jong-Nam;Kim, Wan-Yeong
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.10a
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    • pp.267-270
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    • 2005
  • 유기셀레늄급원을 달리하여 쇠고기 육색 안정성에 미치는 영향을 분석한 결과는 다음과 같다. Myoglobin의 함량은 대조구와 시험구에서 각각 6.39%, 14.18%로 대조구가 시험구에 비하여 낮은 결과를 보였으며, Oxy-Myoglobin의 함량은 반대로 대조구 89.07%, 시험구 83.47%로 시험구가 대조구에 비하여 낮은 결과를 보였다(p<0.05). 그러나 Met-myoglobin 함량은 대조구가 4.56%이였고 시험구가 2.35%로 대조구가 높은 결과를 보였다. 보다 정확한 결과를 평가하기 위해서는 시료를 Met화 시킨 후 측정해 볼 필요성이 대두되어 도축후 $4^{\circ}C$에서 14일 및 21일간 숙성한 시료를 $20^{\circ}C$에서 48시간 산화시킨 후 측정 육색소 화학적 조성을 비교한 결과, 육색소 화학적 조성을 비교한 결과로 Myoglobin 함량은 저장 14일차와 21일차에서 유의적인 차이를 보이지 않았으나, Oxy- myoglobin은 저장 14일차와 21일차 모두 유기셀레늄 강화 버섯 폐배지 급여구가 대조구와 무기셀레늄 급여구에 비하여 높은 결과를 보였다. Met-myoglobin함량에 있어서는 대조구와 무기셀레늄구가 유기 셀레늄구와 유기셀레늄강화 버섯 폐배지 급여구에 비하여 높은 결과를 보였다(p<0.05). 유기셀레늄 강화 버섯 폐배지 급여구가 대조구나 유기셀레늄구에 비하여 Oxy-myoglobin production이 유의적으로 높았으며, Met-myoglobin Activity는 유기 셀레늄 급여구가 가장 높았으며, 그 다음으로는 유기셀레늄강화 버섯폐배지 급여구가 높았다(p<0.05). 이러한 결과는 소매상품 으로 제조 판매시 Oxy-Mb이 Met-Mb으로의 전환을 억제하여 이상적인 육색을 장시간 유지할 수있을 것으로 판단된다.조직감과 염도에서 매우 좋게 평가되었다. 이러한 결과는 제조 가능한 식염첨가최저수준은 0.5%이상임을 보여주었다. 따라서 로인 햄의 제조에 필요로 되는 식염의 첨가량은 0.5${\sim}$1.5% 범위로 평가된다. 차후의 연구로는 저염 로인 햄의 경우 품질의 저하를 보완할 수 있는 기능성 첨가물이나 가공기법이 필요할 것으로 보인다.97.22로 가장 낮았고, 기타 처리구는 1.19${\sim}$1.59의 처리를 보이고 있는데 비하여, 대조구(100) 대비 증체율에서는 생봉독 처리 2구에서 103.30으로 3.30%가 높았다.양성이 무엇보다 중요하다. 특히 지역자원 활용 소스 중심의 문화관린 산업의 seeds 발굴과 향토상품의 상품화와 네트워크 조직망 구축을 위한 지역중심의 복합 생활문화 공간이 필요할 것이며, 이를 촉진키 위한 mentor academy시스템 접근을 통해 점점 고령화되어 가고 있는 재래시장에 대해 차별적 특성이 반영된 종합적이고 체계적 접근 방법연구가 필요하다./TEX> 자체기술개발, 선진기술 도입, 산업간 및 산업내 기술확산, 국제기술협력 ${\rightarrow}$ 기술혁신의 촉진 ${\rightarrow}$ 총요소생산성과 기업경쟁력(자원 및 역량, 프로세스 경쟁력, 품질경쟁력, 시장경쟁력, 고객성과, 시장성과, 재무성과)의 제고 ${\rightarrow}$ 가격경쟁력(임금, 금리, 물류비용, 환율 등)과 비(非)가격경쟁력(디자인, 에프터서비스, 품질, 운송 등)의 제고 ${\rightarrow}$ 국가경쟁력의 제고 ${\rightarrow}$ 국제수지 흑자 ${\rightarrow}$ 성장 ${\rightarrow}$ 물가 및

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A experimental study on the physiological effects of electrical stimulation treatment of serum myoglobin and aldolase in human body (인체에 적용한 전기자극이 Serum myoglobin과 Aldolase에 미치는 영향에 대한 생리학적 효과)

  • Kim, Soon-Hee;Chon, Ki-Young;Choi, Young-Deok
    • Journal of Korean Physical Therapy Science
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    • v.6 no.3
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    • pp.53-61
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    • 1999
  • Prior studies have revealed that several stimulation to the muscle have released serum myoglobin into the blood vessel and increased aldolase activity. The present authors carried out a study which effect of electrical stimulation treatment (induced a isotonic wrist exerceise) on serum myoglobin(Mb) levels and aldolase(Al) activity were investigated in 6 healthy female. There were four groups of female: 1. no electrical stimulation control: 2. electrical stimulation 10min (EST10'); 3. electrical stimulation 20 min (EST20'); 4. electrical stimulation 30min (EST30'). Each groups is all the same one. Radioimmunoassay and Ultraviolet Spectrophotometry were performed to increased or decreased of serum myoglobin and aldolase. Serum myoglobin significantly increased in electrical stimulated groups[EST10' $(30.20{\pm}5.27ng/ml)$, EST20'$(31.65{\pm}3.96ng/ml)$, EST30'$(31.95{\pm}2.0ng/ml)$] to be compared with control group$(24.43{\pm}2.20ng/ml)$. Aldolase significantly increased in electrical stimulated groups [EST10' ($6.85{\pm}1.17$ Sigma U/mL), EST20'($6.70{\pm}1.46$ Sigma U/mL), EST30'($6.56{\pm}1.01$ Sigma U/mL)) to be compared with control group($5.03{\pm}1.86$ Sigma U/mL). The results of this study show that isotonic exercise result in electrical stimulation treatment increased serum myoglobin content and aldolase activity. In conclusion, our results support that stimulation release serum myoglobin and increase aldolase activity.

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Quantitative Label-free Biodetection of Acute Disease Related Proteins Based on Nanomechanical Dynamic Microcantilevers

  • Hwang, Kyo-Seon;Cha, Byung-Hak;Kim, Sang-Kyung;Park, Jung-Ho;Kim, Tae-Song
    • JSTS:Journal of Semiconductor Technology and Science
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    • v.7 no.3
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    • pp.151-160
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    • 2007
  • We report the label-free biomolecules detection based on nanomechanical micro cantilevers operated in dynamic mode for detection of two marker proteins (myoglobin and creatin kinase-MB (CK-MB)) of acute myocardical infarctions. When the specific binding between the antigen and its antibody occurred on the fuctionalized microcantilever surface, mechanical response (i.e. resonant frequency) of microcantilevers was changed in lower frequency range. We performed the label-free biomolecules detection of myoglobin and CK-MB antigen in the low concentration (clinical threshold concentration range) as much as 1 ng/ml from measuring the dynamic response change of micro cantilevers caused by the intermolecular force. Moreover, we estimate the surface stress on the dynamic microcantilevers generated by specific antibody-antigen binding. It is suggested that our dynamic microcantilevers may enable one to use the sensitive label-free biomolecules detection for application to the disease diagnosis system based on mechanical immuno-sensor.

$^{13}C$ NMR Analysis for the Characterization of Heme Electronic/Molecular Structure in Horse Myoglobin Cyanide (Myoglobin 시안 단백질에 포함된 Heme에 대한 전자 및 분자구조 규명을 위한 $^{13}C$ NMR분석)

  • Lee, Kang-Bong;Kweon, Jee-Hye;Lee, Ho-Jin;Kim, Young-Man;Choi, Young-Sang
    • Analytical Science and Technology
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    • v.11 no.1
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    • pp.73-78
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    • 1998
  • The reverse detection heteronuclear multiple quantum coherence, HMQC study of metcyano complex of horse myoglobin(MbCN) has provided the complete assignment of hyperfine shifted resonances of heme carbons attached with proton(s). The application of HMQC experiment to the paramagnetic low-spin MbCN gives clear $^1H$ and $^{13}C$ coherences for the paramagnetic amino acid residues as well as heme side chains, and can be extended to the low-spin paramagnetic hemoprotein derivative for the assignment of natural abundance $^{13}C$ resonances. This assignment strategy can avoid possible ambiguities that may result from the sole utilization of $^1H$ nuclear Overhauser effect for the assignment of heme $^1H$ signals resonating in the diamagnetic region. The resulting 2,4-vinyl ${\alpha}$-carbons and 7-propionate ${\beta}$-carbon follow anomalous anti-Curie behavior, and are indicative of incoplanarity with heme plane. Magnetic/electronic asymmetry of heme induced by proximal histidine(His) makes spread that the hyperfine shifted heme carbon resonances over the range of 250 ppm at $25^{\circ}C$. These heme carbon resonances would be the much more sensitive probe than those of proton resonances in analyzing the nature of heme electronic structure of myoglobin.

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Relationship between angiotensin-converting enzyme gene polymorphism and muscle damage parameters after eccentric exercise

  • Kim, Jooyoung;Kim, Chang-Sun;Lee, Joohyung
    • Korean Journal of Exercise Nutrition
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    • v.17 no.2
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    • pp.25-34
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    • 2013
  • This study was conducted to investigate the relationship between ACE gene polymorphism and muscle damage parameters after eccentric exercise. 80 collegiate males were instructed to take an eccentric exercise with the elbow flexor muscle through the modified preacher curl machine for 2 sets of 25 cycles (total 50 cycles). The maximal isometric strength, muscle soreness, creatine kinase (CK), and myoglobin (Mb) were measured before exercise, and 0, 24, 48, 72, and 96 hrs after exercise. The result showed that after the eccentric exercise, the maximal isometric strength significantly decreased by more than 50% (p < 0.001) and the muscle soreness, CK, and Mb significantly increased compared to those before the exercise (p < 0.001). The ACE gene polymorphism of the subjects was classified using real-time polymerase chain reaction (real-time PCR). The result showed that it consisted of 38 cases of type II (46.4%), 33 cases of type ID (43.4%), and 9 cases of type DD (10.2%). The Hardy-Weinberg equilibrium for ACE gene polymorphism was shown to have p = 0.653, which showed that each allele was evenly distributed. Although significant differences in the changes in the maximal isometric strength, muscle soreness, CK, and Mb were found according to time course (p < 0.001), no significant differences in the changes in the maximal isometric strength, muscle soreness, CK, and Mb were found according to ACE gene polymorphism. Furthermore, no significant difference in the changes in the muscle damage parameters was found according to interaction between ACE gene polymorphism and time course (p > 0.05). In conclusion, the level of the muscle damage parameters changed in the injured muscle after eccentric exercise, but these changes in the muscle damage parameters were not affected by ACE gene polymorphism. The result of this study indicates that ACE gene is not a candidate gene that explains muscle damage.