• Title, Summary, Keyword: Hemoglobin

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Effect of Pretense (Subtilisin Carlsberg) on the Removal of Blood Protein Soil (II) -The Detergency of Hemoglobin from Cotton Fabics- (Protease (Subtilisin Carlsberg) 가 혈액 단백질 오구의 제거에 미치는 영향(II) -헤모글로빈 오구포의 세척성-)

  • 이정숙;김성연
    • Journal of the Korean Society of Clothing and Textiles
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    • v.20 no.4
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    • pp.655-666
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    • 1996
  • The effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The relation between the renloval and the hydrolysis of hemoglobin by subtilisin Carlsberg was discussed. The soiled babric was prepared by spotting of hemoglobin solution evenly on the cotton fabric and was denatured by steaming. The soiled fabric was washed by using Terg-0-Tometer at various conditions. The removal efficiency was evaluated by analysis of protein on the fabrics before and after washing by means of copper-Folin method. 1. The removal of hemoglobin was increased in proportion to increasing of the enzyme concentration up to a certain point, but it began to decrease above the point. 2. The hemoglobin was removed effectively by adding of subtilisin Carlsberg, and more effectively removed by adding of AOS in the enzyme solution. 3. The removal of hemoglobin deviated from the first order reaction in detergency. 4. The renloval of hemoglobin was highest at $50^{\circ}C$ in detergency, Even at low temperature the removal efficiency of enzyme was relatively higher compared with the hydrolysis of hemoglobin by the enzyme. However the removal of hemoglobin was apparently decreased with the increase of temperature over $60^{\circ}C$. 5. The removal of hemoglobin was relatively high at pH 7.0~8.0 and increased continuously with the increase of pH in detergency 6. In detergency, the removal mechanism of hemoglobin by subtilisin Carlsberg could be explained as follows: Fisrt of all, the enzyme hydrolyzed hemoglobin substrates partially by forming E-S complex at the surface of hemoglobin on the cotton fiber, and decomposed cooperative binding of hemoglobin. Subsequently, the fragments of hemoglobin were easily removed by washing. According as the enzyme penetrated to inner part of hemoglobin gradually, the hemoglobin on the cotton fiber was effectively removed by the repetition of these process. The removal of hemoglobin was more effectively increased by adding both the enzyme and AOS in the washing solution. Therefore, it was regarded that AOS molecules were adsorbed at the hydrophobic surface of denatured hemoglobin, subsequently, decomposed more effectively cooperative binding of hemoglobin, and the fragments of hemoglobin were removed more efficiently by means of the interfacial reaction of AOS.

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Fabrication of Hemoglobin/Silver Nanoparticle Heterolayer for Electrochemical Signal-enhanced Bioelectronic Application

  • Lee, Taek;Yoon, Jinho;Choi, Jeong-Woo
    • Korean Chemical Engineering Research
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    • v.55 no.4
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    • pp.556-560
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    • 2017
  • A hemoglobin/silver nanoparticle heterolayer was fabricated for bioelectronic device with electrochemical signal-enhancement effect. As a device element, a hemoglobin, the metalloprotein, contained the heme group that showed the redox property was introduced for charge storage element. For electron transfer facilitation, a silver nanoparticle was introduced for electrochemical signal facilitation, the hemoglobin was immobilized onto Au substrate using chemical linker 6-mercaptohexanoic acid (6-MHA). Then, the silver nanoparticle was immobilized onto fabricated hemoglobin/6-MHA heterolayers by layer-by-layer (LbL) method. The surface morphology and surface roughness of fabricated heterolayer were investigated by atomic force microscopy (AFM). The redox property of hemoglobin/silver nanoparticle heterolayer was investigated by a cyclic voltammetry (CV) experiment for obtaining an oxidation potential and reduction potential. Moreover, for the assessing charge storage function, a chronoamperometry (CA) experiment was conducted to hemoglobin/silver nanoparticle-modified heterolayer electrode using oxidation and reduction potentials, respectively. Based on the results, the fabricated hemoglobin/silver nanoparticle heterolayer showed that an increased charge storage effect compared to hemoglobin monolayer-modified electrode.

Abnormal Hemoglobin Studies in Koreans (한국인의 이상혈색소에 관한 연구)

  • 노일협
    • YAKHAK HOEJI
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    • v.20 no.1
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    • pp.70-75
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    • 1976
  • Two males and one female in the group of 5020 Korean school children and university students in Seoul and Taejon were found to have a show hemoglobin to normal hemoglobin A. In all three subjects the show component migrated at a rate characterstic of the G hemoglobin. By urea-starch-gel electrophoresis in alkaline pH and Chernoff method ws demonstrated that another 3 cases of abnormal hemoglobin also were beta-chain variants. This was reconfirmed by hybridization experiment with canine hemoglobin. And the results of family test of 3 case of abnormal hemoglobin were heterozygous carrier.

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Hemoglobin variant Found in Koreans (한국인(韓國人)을 대상(對象)으로 한 이상혈색소(異常血色素)의 변이형(變異型)에 관(關)한 연구(硏究))

  • Ro, Ihl-Hyeob
    • Journal of Nutrition and Health
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    • v.3 no.3
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    • pp.161-166
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    • 1970
  • One male in the former group of 2110 Korean males of the Republic of Korea Army stationed Taegu. And two males and one female in the later group of 4590 Korean school children and university students in Seoul and Taejuon were found to have a slow hemoglobin in addition to normal hemoglobin A. In all four subjects the slow component migrated at a rate characteristic of the G hemoglobin. The overall incidence of the variant in the present group of Koreans was low: 4 in 6700 or 0.06 percent. It appears significant that no insistence of hemoglobin E were found among these Korean subjects. Hemoglobin E has been found among numerous ethnic groups of Southeast Asia and the variant most frequently appeared in Chinese subject. By Urea-Starch-Gel Electrophoresis in Alkaline PH and A.I. Chernoff method was demonstrated that another 3 cases of abnormal hemoglobin also were beta-chain variants. This was reconfirmed by Hybridization Experiment with canine hemoglobin. And the results of family test of 3 case of abnormal hemoglobin were heterozygous carrier.

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The Effect of Graft using Acrylic Acid on the Detergency for the Nylon 6 Fabric -Improvement of Hemoglobin Removing Rate on Grafted Nylon- (나일론 6 직물의 아크릴산 그라프트 중합과 그라프트 나일론의 세척성 -그라프트 나일론 직물의 헤모글라빈 오구 세척성 향상-)

  • 오수민;김인영;송화순
    • Journal of the Korean Society of Clothing and Textiles
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    • v.23 no.7
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    • pp.1064-1072
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    • 1999
  • Nylon fabric was grafted for the purpose of the development of detergency against the hemoglobin as a protein soil. By free-radical producing chemical initiator systems the graft using acrylic acid(AA) as a hydrophilic vinyl monomer was performed to change surface energies in the presence of ammonium persulfate(APS) as an initiator and then acrylic acid grafted Nylon was treated with NaOH solution. The surface morphology for Nylon-g-NaAA with changing graft rate were studied by scanning electron microscopy (SEM) The properties of the Nylon such as diameter tenacity elongation contact angle and the hemoglobin removal were also investigated. The diameter of grafted Nylon fiber increased as the graft ratio increased. The tenacity of grafted Nylon also increased with increasing graft ratio up to 15% The elongation however decreased gradually according to graft, The contact angle decreased after graft and alkaline treatment. The amount of hemoglobin on the grafted Nylon increased in proportion to the graft ratio. Hemoglobin was easily removed from grafted Nylon while it was difficult to be removed from ungrafted Nylon. The detergency of hemoglobin for grafted Nylon decreased when the graft ratio exceeded 15% The removal of hemoglobin increased markedly with increasing hemoglobin content and revolution speed. Therefore the removal of hemoglobin was improved due to graft and alkaline treatment.

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Detergency of Fabrics with Changes of Mixed Soil Composition Ratio and Protease (혼합오구의 성분비 변화와 프로테아제에 따른 직물의 세척성)

  • 이정숙;성혜영
    • Journal of the Korean Society of Clothing and Textiles
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    • v.25 no.5
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    • pp.991-1001
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    • 2001
  • This study has examined effects of protease on the removal of hemoglobin and triolein mixed soil with changes of soil content and soil composition from cotton and PET filament fabrics. The results obtained were as follows: The results obtained were as follows: 1) The detergency of PET fabrics was higher than that of cotton fabrics. The removal of hemoglobin was much higher than that of triolein from cotton fabrics, while the removal of hemoglobin was similar to that of triolein from PET fabrics. 2) The removal efficiency of hemoglobin and triolein was improved by protease from cotton and PET fabrics. Especially the removal efficiency of those was remarkably improved from cotton fabrics which the removal of soil was lower than PET fabrics. And the removal of hemoglobin and triolein by adding protease was increased with increase of hemoglobin content of mixed soil from cotton fabrics. 3) With the increase of hemoglobin content of mixed soil, the removal of hemoglobin was drastically increased but the removal of triolein was slightly decreased from cotton and PET fabrics. With the increase of triolein content of mixed soil, the removal of hemoglobin and triolein was decreased from cotton fabrics, but those were generally increased from PET fabrics.

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Thermodynamic Elucidation of Binding Isotherms for Hemoglobin & Globin of Human and Bovine upon Interaction with Dodecyl Trimethyl Ammonium Bromide

  • Bordbar, A.K.;Nasehzadeh, A.;Ajloo, D.;Omidiyan, K.;Naghibi, H.;Mehrabi, M.;Khajehpour, H.;Rezaei-Tavirani, M.;Moosavi-Movahedi, A.A.
    • Bulletin of the Korean Chemical Society
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    • v.23 no.8
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    • pp.1073-1077
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    • 2002
  • Binding of dodecyl trimethylammonium bromide (DTAB) to human and bovine hemoglobin and globin samples has been investigated in 50 mM glycine buffer pH = 10, I = 0.0318 and 300 K by equilibrium dialysis and temperature scanning spectrophotometry techniques and method for calculation of average hydrophobicity. The binding data has been analyzed, in terms of binding capacity concept $({\theta})$, Hill coefficient (nH) and intrinsic Gibbs free energy of binding $({\Delta}Gbv).$ The results of binding data, melting point (Tm) and average hydrophobicity show that human hemoglobin has more structural stability than bovine hemoglobin sample. Moreover the results of binding data analysis represent the systems with two and one sets of binding sites for hemoglobin and globin, respectively. It seems that the destabilization of hemoglobin structure due to removal of heme group, is responsible of such behavior. The results indicating the removal of heme group from hemoglobin caused the depletion of first binding set as an electrostatic site upon interaction with DTAB and exposing the hydrophobic patches for protein.

A Study on The Relationship Between Intraoperative Neuromonitoring and Hemoglobin Changes

  • Lee, Kyuhyun;Kim, Jaekyung
    • International journal of advanced smart convergence
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    • v.9 no.4
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    • pp.8-15
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    • 2020
  • This study was conducted in order to determine the effect of intraoperative hemoglobin changes on intraoperative neuromonitoring (IONM). This was a retrospective study that included 339 participants who underwent cerebrovascular surgery. We compared anesthetic agents, intraoperative hemoglobin, hematocrit, blood transfusion, and blood loss. We examined motor evoked potential and sensory evoked potential to patients. There were significant differences in hemoglobin changes, bleeding levels, transfusion, anesthesia time, and postoperative mobility disorders. Moreover, compared with patients who received transfusions, those who did not receive transfusion had a lower average hemoglobin level, as well as a higher bleeding amount, and a need of higher anesthesia time and anesthetic dose. Also, we found vasospasm occurred while surgery can bring adverse results after operation. This study showed that an intraoperative decrease in hemoglobin levels affects the function of cerebral perfusion, which could result in abnormal nerve monitoring results. However, as this study could not find a relation of anesthetics to IONM, there is a need for further research regarding the association between anesthetics and hemoglobin changes and IONM.

Vibrio vulnificus Metalloprotease VvpE has no Direct Effect on Iron-uptake from Human Hemoglobin

  • Sun, Hui-Yu;Han, Song-Iy;Choi, Mi-Hwa;Kim, Seong-Jung;Kim, Choon-Mee;Shin, Sung-Heui
    • Journal of Microbiology
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    • v.44 no.5
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    • pp.537-547
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    • 2006
  • This study was designed to determine whether or not Vibrio vulnificus metalloprotease VvpE can promote iron uptake via the proteolytic cleavage of human hemoglobin. We found that V. vulnificus utilized hemoglobin as an iron source more efficiently via the vulnibactin-mediated iron-uptake system than via the HupA-mediated iron-uptake system and, of the proteases produced by V. vulnificus, VvpE was found to be the only protease capable of destroying hemoglobin. However, VvpE expression, on both the transcriptional and protein levels, was suppressed in iron-limited media. However, vvpE transcription, but not extracellular VvpE production, was reactivated by the addition of hemoglobin or inorganic iron into iron-limited media. Moreover, vvpE transcription began only in the late growth phase when V. vulnificus had already consumed most of the iron for growth. In addition, neither vvpE mutation nor in trans vvpE complementation affected the ability of V. vulnificus to acquire iron or to grow in iron-limited media or in cirrhotic ascites containing hemoglobin. Hemoglobin added into iron-limited media was not destroyed, but gradually formed an insoluble aggregate during culture; this aggregation of hemoglobin occurred regardless of vvpE mutation or complementation. These results indicate that VvpE is not required for efficient iron uptake from hemoglobin. On the contrary, hemoglobin or iron is required for efficient vvpE transcription. In addition, a discrepancy exists between vvpE transcription and extracellular VvpE production in iron-limited media containing inorganic iron or hemoglobin, which suggests that additional unknown posttranscriptional events may be involved in the extracellular production of VvpE.

Pharmacokinetics of PEG-Hemoglobin SB1, a Hemoglobin-Based Oxygen Carrier, after Its Intravenous Administration in Beagle Dogs

  • Kwon, Oh-Seung;Chung, Uoo-Tae;Chung, Youn-Bok
    • Archives of Pharmacal Research
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    • v.27 no.2
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    • pp.259-264
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    • 2004
  • The purpose of the present study was to investigate the pharmacokinetics of PEG-hemoglobin SB 1, a modified bovine hemoglobin with polyethylene glycol, after its single and multiple administration in beagle dogs. For this purpose, the analytical method of free hemoglobin in the plasma was developed and validated. Excellent linearity ($r^2$=0.999) was observed in the calibration curve data, with the limit of quantification of 0.005 g/dL. The precision and the deviation of the theoretical values for accuracy were always within $\pm$15% in both the between-and the within-day results. The method was tested by measuring the plasma concentrations following intravenous administration to beagle dogs and was shown to be suitable for pharmacokinetic studies. In a single dose study, the plasma half-life (t$_{1}$2/) increased and the total body clearance (Cl$_{t}$) decreased with the dose (i.e., 0.017 to 0.75 gHb/kg as PEG-hemoglobin SB1) in both sexes. The volume of distribution at steady-state (Vd$_{ss}$ ) showed no difference with the dose. In contrast, the values of t$_{1}$2/, CL$_{t}$ and the area under the plasma concentration-time curve (AUC) after the multiple dose were significantly different from those of the single dose administration. The values of t$_{1}$2/ in the multiple administration were about two times higher-than that of the single dose. As a result, t$_{1}$2/ of hemoglobin after the administration of PEG-hemoglobin SB1 was about 15-30 h, indicating the PEG modification of the hemoglobin lead to a prolongation of plasma concentration of the protein. Therefore, these observations suggested that the PEG modification of hemoglobin is potentially applicable in the hemoglobin-based therapeutics.tics.