• 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.

• 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.

• 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.

• 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.

• 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.

• 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.

• 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.

• 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.

• Korean Journal of Veterinary Research
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• v.38 no.4
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• pp.946-956
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• 1998

Fifteen mongrel dogs (14 male and 1 female) were injected intravenously with 30mg of streptozotocin and 50mg of alloxan monohydrate per kilogram of body weight to induce diabetes mellitus. Before treatment with streptozotocin and alloxan fasting serum glucose concentration was determined every other day or thrice a week (Monday, Wednesday, Friday) for 3 months. Among 15 dogs 4 dogs developed diabetes mellitus and survived more than 9 weeks without injection of insulin. After treatment fasting serum glucose and hemoglobin $A_1$ concentrations of the 4 dogs were determined every other day or thrice a week. Fasting serum glucose concentration increased acutely from 24 hours after treatment and then showed severe fluctuation. Hemoglobin $A_1$ concentration increased gradually until 7~9 weeks after treatment and then showed very slow increase afterwards. Correlation of hemoglobin $A_1$ to fasting glucose concentration was relatively weak(r = 0.10~0.80). Hemoglobin $A_1$ and fasting glucose concentration of preceding 7 week showed very high correlation (r = 0.98~0.99). It was indicated that hemoglobin $A_1$ concentration in chemically induced diabetic dogs reflects mean glucose concentration of preceding 7~9 weeks.

• Journal of the Korean Society of Clothing and Textiles
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• v.20 no.3
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• pp.550-559
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• 1996

The Effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The hydrolysis characteristics of subtilisin Carlsberg was examined by electrophoretic techniques. The fragmentation patterns of hemoglobin were analyzed by SDS-PAGE. The hydrolysis efficiency was evaluated by analysis of protein bands shown on gels before and after hydrolysis by using densitometer. 1. The hydrolysis of hemoglobin by subtilisin Carlsberg was increased markedly with the increase of the enzyme concentration. 2. The hydrolysis of hemoglobin by subtilisin Carlsberg was effectively increased in proportion to increasing of the hemoglobin concentration up to a certain point, but it began to decrease above the point. 3. The hydrolysis of hemoglobin by subtilisin Carlsberg followed the first order kinetics, yielding a rate constant of $4.05\time10^{-4}S^{-1}s$. 4. The hydrolysis of hemoglobin by subtilisin Carlsberg was highest at $50^{\circ}C$ and was decreased markedly at $80^{\circ}C$. 5. The hydrolysis of hemoglobin was comparatively low at pH 7.0~8.0, and highest at pH 11.0.