• Nuclear Engineering and Technology
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• v.3 no.3
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• pp.141-147
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• 1971

In iodine-131 labelling of iodocompounds such as tetrachloro-P-tetraiodo R-fluorescein, sodium orthoiodohippurate and a non-iodocompound, human serum albumin (HSA), the labelling rates and yields are accurately compared with each other. The reaction systems conducted for each compounds were different conditions: sodium iodide-$^{131}$ I containing reducing agent, sodium iodide-$^{131}$ I free from reducing agent, and sodium iodide-$^{131}$ I free from reducing agent but containing considerable amount of iodide-$^{131}$ I etc. The labelling yields were generally poor; 10% in the case of using sodium iodide-$^{131}$ I containing redoing agent, and 50~60% in the case of using sodium iodide-$^{131}$ I free from reducing agent but containing considerable amount of iodide-$^{131}$ I. However, fair yields were obtained in the case of using sodium iodide-$^{131}$ I free from reducing agent and mostly in the form of iodide-$^{131}$ I. The reaction entities involved in these reactions are also briefly discussed.

• BMB Reports
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• v.32 no.4
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• pp.350-357
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• 1999

At concentrations of 1 mM, the protective effects of carnosine and related compounds including anserine, homocarnosine, histidine, ${\beta}$-alanine were investigated against copper-catalyzed oxidative damage to deoxyribose, ascorbic acid, human serum albumin, liposome, and erythrocytes. Carnosine and anserine reduced Cu (II) to bathocuproine-reactive Cu (I) in a time- a and a dose-dependent manner while the others did not. Carnosine reduced 86% of $100\;{\mu}M$ Cu (II) in 60 min. Carnosine, homocarnosine, anserine, and histidine inhibited copper-catalyzed deoxyribose degradation by 75, 66, 65, and 45%, respectively. In the presence of $1\;{\mu}M$ Cu (II), carnosine and related compounds inhibited ascorbic acid oxidation by 55-85% after incubation for 20 min. In the presence of 0.15 mM ascorbic acid and 0.8 mM $H_2O_2$, carnosine, anserine, homocarnosine, and histidine inhibited copper-catalyzed oxidation of human serum albumin by 41, 21, 29, and 24%, respectively, as determined by carbonyl formation. These compounds also significantly inhibited copper-catalyzed liposomal lipid peroxidation as measured by malondialehyde and lipid hydroperoxides. Carnosine, anserine, homocarnosine, and histidine inhibited hemolysis of bovine erythrocytes induced by 0.1 mM Cu (II). These results suggest that histidine-containing dipeptides may play an important role in protecting against free radical-mediated tissue damage.

• Journal of Microbiology and Biotechnology
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• v.18 no.9
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• pp.1599-1605
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• 2008

Biodistribution and lymphoscintigraphy of cyclosporine A (CyA) and technetium-99m ($^{99m}Tc$) were studied using ${^99m}Tc$-labeled dextran acetate (DxA) including CyA. DxA particles were prepared from dextran with acetic anhydride, and CyA was loaded into them. Lymphatic delivery of ${^99m}Tc$-labeled DxA particles containing CyA was evaluated after subcutaneous injection into the foot pad of rats and compared with those of ${^99m}Tc$-labeled human serum albumin (HSA). The labeling efficiency of CyA-loaded ${^99m}Tc$-DxA particles was about 95% at 30 min. The labeling efficiency maintained stably above 80% for 12 h. The percent injected dose (%ID) of CyA-loaded ${^99m}Tc$-DxA was similar to that of ${^99m}Tc$-HSA at the inguinal lymph node after 40 min. The CyA-loaded ${^99m}Tc$-DxA could be as well distributed as ${^99m}Tc$-HSA through the lymph node. The DxA particles could steadily distribute the CyA as well as the ${^99m}Tc$ radiolabeling through the lymph node.

• KSBB Journal
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• v.18 no.2
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• pp.100-106
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• 2003

An on-line frontal analysis HPLC system was developed to determine the unbound concentration of (S)-perillyl alcohol, an potential anti-cancer agent, in human serum albumin (HSA) solution, The analysis was performed on a Develosil 100 Diol 5 (10 cm x 4.6 mm I.D.) high-performance frontal analysis (HPFA) column. Sodium phosphate solution was used as the mobile phase (pH 7.4, ionic strength 0.17) at a flow rate of 1 $m\ell$/min. UV wavelength was set at 205 nm. A injection volume of 600${mu}ell$ was chosen to ensure the compound eluted formed a zonal peak with a plateau. By Scatchard analysis, it was found that the binding constant(K) and binding number(n) of (S)-perillyl alcohol to molecular HSA were 2.05 x $10^6$ [$M{-1}$], 0.00428, respectively.

• BMB Reports
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• v.39 no.5
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• pp.530-536
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• 2006

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from $25^{\circ}C$ to $55^{\circ}C$ induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. $42^{\circ}C$. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at $45^{\circ}C$ and $35^{\circ}C$ reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at $45^{\circ}C$ compared to $35^{\circ}C$, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.

• Membrane Journal
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• v.8 no.1
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• pp.50-58
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• 1998

Protein affinity membranes were prepared via coating of chitosan gel on the porous flat and hollow-fiber polysulfone membranes, followed by the immobilization of the reactive dye (Cibacron Blue 3GA) to the chitosan gel. Maximum protein binding capacity of these affinity membranes was about 70 $\mu{g/cm}^2$. Using the affinity flat membrane module, the elution chromatography of human serum albumin (HSA) was performed to determine the optimum condition of eluent buffer. The optimum condition of eluent was the universal buffer solution of 0.06 M concentration containing 1 M KCl at pH 10. For the frontal chromatography of HSA using the flat module, the dynamic protein binding capacity was rapidly decreased from the equilibrium values with increasing flow rate and HSA concentration of the loading solution. However, in the case of hollow-fiber module, the dynamic binding capacity was maintained an equilibrium value without depending on the operating conditions. These results showed that the hollow-fiber module was more effective than the flat module as an affinity chromatography column.

• Development and Reproduction
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• v.6 no.1
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• pp.31-35
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• 2002

The major urinary proteins(MUPs) of mice that bind hydrophobic molecules known as pheromones are regulated in part by the actions of growth hormone. The expression of the MUPs was therefore investigated in transgenic mice that express a human growth hormone-releasing factor gene from a metallothionein gene promoter(MT-GRF) and as a result have elevated growth hormone levels. MUPs were severely down-regulated in the urine of these animals compared to normal mice or to control transgenic mice expressing another gene(the inhibin a subunit) from the same metallothionein promoter(MT-Inh) and more MUPs disappeared in male mice than female ones. MUPs were also down-regulated in the urine of the UT-GRF-injected mice. In addition, it was observed that the urine of the MT-GRF mice included a high molecular weight protein that co-migrates with the major serum protein albumin, indicating an impairment in glomerular filtration within the kidney. The urinary loss of serum proteins was more severe in male MT-GRF mice than female ones. Thus the overexpression of human GRF mimics changes observed in MUP protein expression and glomerular function in other models of growth hormone hypersecretion with sex-dependent differential effects.

• YAKHAK HOEJI
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• v.53 no.3
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• pp.101-106
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• 2009

Recombinant interferon alpha-2a is an active formula for the treatment of various cancer cells like malignant melanoma and a variety of virus infection diseases like acute or chronic hepatitis. The bioassay system based on the measurement of virus inhibitory activity by interferon has been used for interferon analysis with low repeatability. Here, we developed the HPLC assay to measure reproducibly interferon alpha-2a protein content which is replaceable to the reported bioassay. This method separated interferon alpha-2a from its oxidized forms and human serum albumin used as excipients. The regression coefficient using interferon alpha-2a EP CRS is more than 0.9 in the range from 5 ${\mu}g/ml$ to 200 ${\mu}g/ml$. The recovery result in the range from 15 ${\mu}g/ml$ to 60 ${\mu}g/ml$ is $97{\sim}104%$ and the precision is $0.2{\sim}1.7%$. The interferon alpha contents of 5 products are about 30 ${\mu}g/ml$.

• Bulletin of the Korean Chemical Society
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• v.34 no.11
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• pp.3243-3248
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• 2013

The tissue inhibitor of metalloproteinase-2 (TIMP-2) inhibits matrix metalloproteinases activity and modulates cellular proliferation and apoptosis. The human serum albumin-TIMP-2 with folic acid conjugate (termed HT2-folate) was synthesized to promote uptake through folate receptors (FRs), and a corresponding radio-labeled compound was prepared for tumor diagnosis by positron emission tomography (PET). $^{68}Ga$-NOTA-HT2-folate was synthesized from $^{68}Ga$ and the NOTA chelator with HT2-folate. The fusion protein was identified using MALDI-TOF mass spectrometry. The radioligand was prepared with a high radiochemical yield. Cell-surface association of $^{68}Ga$-NOTA-HT2-folate significantly increased over time in FR-positive tumor cells. In animal PET and biodistribution studies, tumor uptake was very high as early as 1 h after radioligand injection. Folate conjugation enhanced the selective receptor-targeting efficacy of HT2 in FRexpressing tumors, and its radioligand will be useful as an in vitro tool and for in vivo tumor diagnosis by PET imaging.

• Parasites, Hosts and Diseases
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• v.43 no.4 s.136
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• pp.157-160
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• 2005

A 29kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required.