• 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.

• 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.

• 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.

• Journal of Life Science
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• v.27 no.6
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• pp.632-639
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• 2017

Mature haptoglobin (Hp) is a plasma glycoprotein and acts as an antioxidant by scavenging cell-free hemoglobin (Hb). Prohaptoglobin (proHp) is an unprocessed Hp precursor which is present a little in circulation. However, the biological function of proHp remains unknown. To investigate the structural and functional differences between proHp and Hp, we prepared recombinant proHp isoforms and compared their sialic acid content and Hb-binding capacity with those of mature isoforms. When proHp samples were analyzed by Western blot under non-reducing conditions, proHp1 was detected as one band of approximately 130 kDa and proHp2 as multiple bands >200 kDa, in the manner of mature Hp1-1 and Hp2-2, respectively. On the native polyacrylamide gel under non-reducing and non-denaturing conditions, both proHp isoforms migrated more slowly than their mature Hp counterparts. In addition, the lectin-based ELISA assay demonstrated that the content of sialic acid in proHp1 and proHp2 was much less than in Hp1-1 and Hp2-2. The Hb-binding capacity of proHp was also lower than those of mature Hp. These findings indicate that proHp and Hp are similar in the size and polymerization pattern, but different in sialic acid content and Hb-binding activity. It suggests precursor proHp may exert different functions in circulation than does mature Hp.

• Journal of Nutrition and Health
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• v.30 no.8
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• pp.1009-1017
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• 1997

This study was designed to assess the iron nutritional status and growth development of children provided with and without the national school -lunch program(NLSP). The subjects consisted of 590 elementary school children (313 boys, 277 girls) in the 2nd, 4th and 6th grades provided with (n=390) and without (n=200) NSLP. anthropometric measurements were taken for body weight, height, triceps skinfold thickness and body fat percentage. Nutrient intakes were assessed by a modified 24 -hour recall method. Fastinig blood samples were obtained and analyzed for hemoglobin concentration, hematocrit, serum iron and total iron binding capacity. The results obtained are summarized as follows. No significant differences between children provided with and without NSLP were found in height and body weight, but triceps skinfold thickness and body fat(%) were significantly higher in children without NSLP than in those with NSLP. There was no significant difference in hemoglobin concentration and hematocrit between children provided with and without NSLP. However, serum iron concentration and transferrin saturation were higher in the children provided with NSLP(81.9$\mu\textrm{g}$/dl and 22.8%) than in the children without NSLP(73.1$\mu\textrm{g}$/dl and 20.9%). When comparing iron and vitamin C intakes , iron intake was significantly higher in children provided with school-lunch, but vitamin C intake was significantly higher in children provided without school-lunch. Percentages of iron -deficient anemia in underweight, normal and obese children when judged by total iron binding capacity were 14.9%, 12.5% and 25.8% respectively.

• The Korea Journal of Herbology
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• v.35 no.4
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• pp.1-8
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• 2020

Objectives : Angelicae gigas, A. sinensis and A. acutiloba are three types of plants used as Angelicae Radix (Dang-Gui). Many doctors of Korean medicine want to know the difference in clinical use of these three species. This study aimed to compare the hemoglobin-related activity of the extracts of Angelicae gigas, A. sinensis and A. acutiloba roots by measuring the intensity of binding oxygen to hemoglobin using Raman spectroscopy. Methods : Hemoglobin activity was measured by chemical analysis and Raman spectroscopy to compare the pharmaceutical efficacy of three Angelica root extracts. The oxygenated hemoglobin intensity, blood decursinol and acetylcholinestrase(AChE) concentration in mice were measured. In addition, the effects of three Angelica root extracts on oxygenated hemoglobin intensity, decursinol and AChE concentration in red blood cells (RBC) from human were also investigated. Results : The contents of decursin, decursinol and decursinol angelate, which affected physiological activity and RBC properties, were higher in the extract of A. gigas root than in those of A. sinensis and A. acutiloba roots. Moreover, oxygenated hemoglobin intensity in the A. gigas extract was higher than that of other two species in the blood of mice and human RBCs. Also, the blood decursinol and AChE concentrations of A. gigas root extract were higher than that of A. sinensis and A. acutiloba roots. Conclusions : These results suggest that A. gigas is more effective in treating disease related oxygen deficiency in RBC deformation under oxidative stress.

• 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.

• Journal of Nutrition and Health
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• v.36 no.7
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• pp.729-735
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• 2003

This study was performed to evaluate the effect of iron supplement for 4 weeks on iron status, immunity, and antioxidant status of national female soccer players (n = 25). This study was performed at summer hard training period right before competition. A single blind design was used to divide the subjects into iron-supplement (IS) or placebo group (P). Iron-supplement group was supplemented with iron (40 mg/d) for 4 weeks. The mean age of the subjects was 23.3 $\pm$ 2.5 years old. Mean height and body weight of the subjects were 164.4 $\pm$ 5.7 em and 57.4 $\pm$ 4.6 kg, respectively. The mean carrier as soccer player was 11.0 $\pm$ 2.6 years and mean training time was 7.0 $\pm$ 1.3 hr/day. The mean hemoglobin, hematocrit, total iron binding capacity and ferritin concentrations before iron supplementation were not different between two groups. After 4 weeks of summer training and iron supplementation, serum ferritin level was significantly increased only in IS group after supplementation. Mean corpuscular volume and total iron binding capacity were significantly decreased in both groups. Meanwhile, hemoglobin and red blood cell count were significantly lowered only in placebo group. The IgM concentration increased significantly in both groups, but IgG concentration had increasing tendency only in IS group (p < 0.064). Therefore, iron supplementation during hard training period may be helpful to improve work capacity of the athletes by improving ferritin status and humoral immune responses.

• Toxicological Research
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• v.13 no.3
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• pp.257-263
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• 1997

Pentachlorophenol(PCP) which ks widely used in wood preservation, pulp and paper mills, has led to a substantial envirortmental contamination. To get the reliable data for the effective health risk assessment with PCP, covalent binding potential of PCP to cellular macromolecules and glutathione(GSH) was investigated after intraperitoneal administration of $^{14}C-PCP$ to rats. PCP metabolites were able to bind covalently to serum albumin and hepatic protein in a dose- and time-dependent manner. Hepatic protein adducts of PCP metabolites were increased as a function of cytochrome P-450 activities, whereas, albumin adducts significantly decreased. Covalent binding of PCP metabolites with DNA or hemoglobin was not observed. GSH levels in liver tissue decreased over 12hrs, however, the level was recovered after 48hrs. Tetrachloro-1,4-benzoquinone (1,4-TCBQ), one of the most reactive PCP metabolites, conjugated with GSH very rapidly. Base on our results, we could conclude that PCP metabolized to reactive electrophilic metabolites by cytochrome P-450 isoenzymes and conjugated rapidly with neighboring protein or nonprotein sulfhydryl before reacting with DNA or hemoglobin. We propose that albumin adducts and mercapturic acids of PCP metabolites can be used good biomarker of recent PCP exposure.

• Journal of Nutrition and Health
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• v.32 no.7
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• pp.793-801
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• 1999

The purposes of this study are to assess iron status in mothers and their newborn infants at birth and to analyze the influence of maternal iron status on their newborn babies. Venous bloods samples were drawn from 144 pregnant women just before delivery and cord bloods of their newborn babies were collected immediately after birth for measurement of hemoglobin, hematocrit, serum iron, ferritin, total binding capacity and transferrin saturation. The values of hemoglobin and hematocrit were significantly lower in the mothers(10.9$\pm$1.43g/dl and 33.7$\pm$3.67%) than in their newborn infants(14.7$\pm$1.43g/dl and 45.3$\pm$4.76%)(p<0.0001). At delivery, serum iron levels in cord blood were about twice as high as those in the maternal blood, and serum ferritin levels in the cord blood were about four times higher than those in the maternal blood. The serum ferritin levels of multigravidas were higher than those of primigravidas,. but there was no difference between the serum ferritin levels of their infants. The serum ferritin levels of the mothers and their infants were higher in maternal group with iron supplement regularly than in other maternal group without iron supplement during pregnancy. Among the mothers, 26.4% had a serum ferritin levels below 12ng/ml(i.e. depleted iron stores)and 78.9% had a hemoglobin below 12g/dl(i.e.iron deficient anemia). When the maternal group was classified according to their serum ferritin levels by 9ng/ml, 12ng/dl or 20ng/ml, there was no significant difference in the iron status of their newborn infants among the three groups. The hemoglobin and serum ferritin levels of the mothers were well correlated with those of their babies. The maternal hemoglobin values negatively correlated with infant birth weight. It is possible that the demands of iron of the mother might be increased in the case of a newborn infant of greater size. The results of this study provide useful information regarding establishment of RDA for iron in pregnant women and guidance about the need for iron supplement during pregnancy.