• The Korean Journal of Physiology
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• v.26 no.1
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• pp.37-44
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• 1992

The encapsulation of the Purified bovine hemoglobin with Phospholipids obtained from egg folk was performed using a rotary vacuum evaporator. The prepared Hb-containing liposome (hemosome) had good properties as artificial red blood cell. The shape and size of the hemosomes were measured by a phase contrast microscope and image analyzer. The function of the hemosome as oxygen carrier was tested by measuring oxygen saturation curve with blood gas analyzer and infusing it into rats. The prepared hemosome was 1.184 + 0.423 ${\mu}m$ in diameter and round in shape. $P_{50}$ value of the hemosome solution was 28 mmHg. The synthesized red cells seem to function as oxygen carrier, because the severely bled rats were prolonged in their life by transfusion of the hemosome solution containing bovine hemoglobin.

• Proceedings of the Korean Vacuum Society Conference
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• 2016.02a
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• pp.208.2-208.2
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• 2016

Many researchers have paid attention to the studies on the interaction between non-thermal plasma and aqueous solutions for biomedical applications. The gas composition in the plasma is very important. Oxygen and nitrogen are the main gases of interest in biological applications. Especially, we focus on the oxygen concentration. In this experiment, we studied the role of oxygen concentration in plasma induced chemical reactions in solution. At first, the amount of ions are measured according to changing the oxygen concentration. And we checked the relationship between these ions and pH value. Secondly, when the oxygen concentration is changed, it identified the type and amount of radical generated by the plasma. In order to confirm the effect of these chemical property change to biological material, hemoglobin and RBCs are chosen. RBCs are one of the common basic biological cells. Thirdly, when plasma treated according to oxygen concentration in nitrogen feeding gas, oxidation of hemoglobin and RBC is checked. Finally, membrane oxidation of RBC is measured to examine the relation between hemoglobin oxidation and membrane damage through relative hemolysis and Young's modulus. Our results suggest that reactive species generated by the plasma differsdepending on the oxygen concentration changes. The pH values are decreased when oxygen concentration increased. OH decrease and NO increase are also observed. These reactive species makes change of chemical properties of solution. We also able to confirm that the difference in these reactive species to affect the oxidation of the Hb and RBCs. The Hb and RBCs are more oxidized with the high oxygen concentration conditions. But membrane is damaged more by plasma treatment with only nitrogen gas. It is shown that red blood cells membrane damage and oxidation of hemoglobin are not directly related.

• BMB Reports
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• v.29 no.3
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• pp.261-265
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• 1996

Sheep hemoglobin (SHb) was modified with methoxy-polyethylene glycol (mPEG) to develop a potential blood substitute. mPEG has been used to decrease antigenicity and immunogenicity of foreign proteins. When the mPEG was attached to SHb, the modified hemoglobins showed decreased electrophoretic mobility on SDS-PAGE and decreased free amino groups. When the remaining free amino groups of mPEG modified SHb were determined by TNBS free amino group titration methods. about 34% of total free amino groups were modified with mPEG. This mPEG-SHb conjugate of 34% amino groups modified showed no precipitation by double immunodiffusion with polyclonal antibodies against SHb. This modified hemoglobin still has oxygen transport activity. So this antigenicity decreased hemoglobin may be used in humans as a potential blood substitute.

• Journal of Microbiology and Biotechnology
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• v.24 no.12
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• pp.1685-1689
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• 2014

Baeyer-Villiger (BV) oxidation of cyclohexanone to ${\varepsilon}$-caprolactone in a microbial system expressing cyclohexanone monooxygenase (CHMO) can be influenced by not only the efficient regeneration of NADPH but also a sufficient supply of oxygen. In this study, the bacterial hemoglobin gene from Vitreoscilla stercoraria (vhb) was introduced into the recombinant Escherichia coli expressing CHMO to investigate the effects of an oxygen-carrying protein on microbial BV oxidation of cyclohexanone. Coexpression of Vhb allowed the recombinant E. coli strain to produce a maximum ${\varepsilon}$-caprolactone concentration of 15.7 g/l in a fed-batch BV oxidation of cyclohexanone, which corresponded to a 43% improvement compared with the control strain expressing CHMO only under the same conditions.

• 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.

• The Korean Journal of Physiology
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• v.24 no.1
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• pp.15-26
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• 1990

Hemoglobin was purified from the outdated human red blood cells. Phospholipids were purified from egg yolk and stored in chloroform. The artificial red blood cells (hemosome) were prepared by encapsulation of hemoglobin with phospholipid mutilayer using rotary vacuum evaporator. The shape and size of hemosomes were measured by phase contrast microscope and image analyzer. The function of hemosomes was tested by measuring oxygen dissociation curve using blood gas analyzer. In order to test whether hemosomes are useful as blood substitute they were infused into rats of which one third of total blood were drawn. The results obtained are summarized at followings. 1) Hemosomes were spherical shape and their mean diameter was 0.7 um. 2) Oxygen dissociation curve of hemosomes showed the same figure as that of normal red blood cells. 3) All rats given 1/3 transfusion with hemosomes survived until sacrificed whereas three of four rats given 1/3 transfusion with saline died within 1 hour and the rest of them died within 24 hours.

• Biomedical Science Letters
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• v.11 no.1
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• pp.85-88
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• 2005

Hemoglobin is oxygen carrier protein within erythrocyte in blood. Apoprotein of this, globin, is synthesized in the cytosol but it's cofactor, heme, is synthesized in the mitochondria. It has not been known very well how globin receives the heme from mitochondria and folds to hemoglobin. In this folding process, the initial structure of globin seems to be very important. A small volume of globin at acid pH was added rapidly into the bulk of an egg phosphatidylcholine $60\%$ liposome, containing hemins, at neutral pH according to the Rapid Dilution method. It was observed that an acid-induced unfolding structure of globin is initially needed to receive hemins from the lipid bilayer of liposomes. Also, this conclusion was confirmed with the absorption spectrum of the refolded globin separated by centrifugation.

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
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• 2003.10a
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• pp.135.1-135
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• 2003

To elucidate the effect of gamma-irradiation on the molecular properties of hemoglobin, the secondary, tertiary structure, and the molecular weight size of the protein were examined after irradiation at 0.5, 1, 5, and 10 kGy. Gamma-irradiation of hemoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross-linking, and aggregation of the polypeptide chains. A SDS-PAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid decreased the degradation and aggregation of proteins by scavenging oxygen radicals that were produced by irradiation. A circular dichroism study showed that irradiation decreased the helical content of hemoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation decreased the emission intensity that was excited at 280 nm.

• Journal of IKEEE
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• v.18 no.1
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• pp.172-178
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• 2014

This paper describes the design technique and the method of analog front-end to measure the saturation of hemoglobin with oxygen sensor. To process the $SpO_2$ value from the sensor, the current data from the sensor should be converted into voltage domain. Designed analog front-end usually converts the current data from the sensor into voltage domain data to pass it on analog-to-digital converter called ADC with a different level of gain characteristics. This circuit was fabricated in a $0.11{\mu}m$ CMOS technology and has 4 level of gain properties. The occupied area is $0.174mm^2$.

• Journal of Dental Anesthesia and Pain Medicine
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• v.21 no.5
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• pp.471-474
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• 2021

Methemoglobinemia is rare. It is classified into two types: congenital methemoglobinemia and acquired methemoglobinemia. Methemoglobin is incapable of binding oxygen, leading to complications such as cyanosis, dyspnea, headache, and heart failure. In the present case, a 35-year-old man with congenital methemoglobinemia underwent general anesthesia for thyroidectomy. The patient was diagnosed with hemoglobin M at 7 years of age. Ventilation was performed with FiO₂ 1.0. Arterial blood gas analysis showed that the pH was 7.4, PaO₂ 439 mmHg, PaCO₂ 40.5 mmHg, oxyhemoglobin level of 83.2%, and methemoglobin level of 15.5%. The patient had a stable course, although cyanosis was observed during surgery.