• The Journal of Pediatrics of Korean Medicine
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• v.11 no.1
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• pp.249-273
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• 1997

Hyunggyeyungyotang has been used for treatment of sinusitis and otitis media in oriental medicine since ancient times. It is reported that Hyunggyeyungyotang has good effects on inflammatory and allergic diseases of otorhinolaryngology in clinical medicine. Kamihyunggyeyungyotang was made by adding several herbs to Hyunggyeyungyotang which has such good effects. To investigate the effects of Hyunggyeyungyotang and Kamihyunggyeyungyotang on inflammatory, algesic and allergic diseases, the author examined the analgesic effect by acetic acid reaction, studied the anti-inflammatory effect through the experiments of the protein thermo-denaturation and circumscribed edema. Besides researched the anti-allergic effect through the vascular permeability response to Chemical Mediator and the delayed type hypersensitivity response to Picryl Chloride. The obtained results were as follows ; 1. In the analgesic effect of Hyunggyeyungyotang and Kamihyunggyeyungyotang extract by acetic acid method, both of the sample groups showed the analgesia, but didn't show useful effect. 2. In the anti-inflammatory effect on the protein thermo-denaturation, the sample groups revealed the inhibitory effect in proportion to concentration as compared with the control group. 3. In the inhibitory action on circumscribed edema induced by Caraggeenin, both of Hyunggyeyungyotang and Kamihyunggyeyungyotang administration showed the significant effect after 4 hours in comparison to the control group. 4. In the delayed type hypersensitivity response to Picryl Chloride, both of the sample groups revealed the significant effects. 5. Both of the sample groups decreased the vascular permeability induced by Histamine in comparison with the control group, but the significancy was admitted in only Hyunggyeyungyotang administration. According to above results, Hyunggyeyungyotang and Kamihyunggyeyungyotang are considered to be used for treament of the inflammatory diseases including sinusitis.

• The Korean Journal of Zoology
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• v.31 no.3
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• pp.157-164
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• 1988

SCK tumor cells were exposed to heat shock or several sulihydryl-reacting agents such as iodoacetamide(IAA), zinc chloride(Zn), and 2-mercaptoethanol(ME). Stress proteins induced by these agents were examined and the relationship between the induction of stress proteins and the production of abnormal proteins was discussed. Based on the present experiments, two classes of intracellular pathways for the induction of stress proteins were defined; one dependent on and the other independent of protein synthesis. The presence of cycloheximide during the induction period blocked the formation of stress proteins in the cells exposed to Zn or ME, but not in those exposed to heat shock or IAA.Therefore, stress protein seems to be induced either by denaturation of pre-existing mature proteins (e.g., heat shock or IAA) or by newly synthesized abnormal proteins(e.g., Zn or ME). In conclusion, it is ilkely that the production of abnormal proteins by stresses triggers stress protein induction. In addition, it was found that the cells exposed to IISP and GRP inducers simultaneously responded to more strong stress among several stresses encountered.

• BMB Reports
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• v.32 no.3
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• pp.317-319
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• 1999

A leucine aminopeptidase has been isolated from the culture medium of the soil fungus, Aspergillus flavus. The enzyme was found to be a glycoprotein, as judged by electrophoresis analysis and the subsequent staining by the periodic acid-Schiff's reagent. Carbohydrate moieties could be cleaved by N-glycosidase, but not by O-glycosidase, indicating that the glucans are linked to the asparagine residue in the protein. Removal of N-glucans was observed without prior denaturation of the protein, implying that the N-glycosidic linkage is exposed and accessible to glycosidase. When the activity of native or deglycosylated enzyme was measured in the presence of various metal ions, removal of carbohydrates increased the aminopeptidase activity of the enzyme.

• Journal of Microbiology and Biotechnology
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• v.13 no.6
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• pp.989-992
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• 2003

Recombinant human tissue plasminogen activator deletion mutein (Reteplase) is a clinically promising thrombolytic drug. Reteplase cDNA was subcloned into a bacteria expression system, and the resultant recombinant was biologically characterized. The Reteplase was expressed in Escherichia coli as an inclusion body, and the downstream processes of the Reteplase inclusion body included denaturation, renaturation, and purification. A protein disulfide isomerase (PDI) was used to assist the refolding of Reteplase, and it was found to increase the refolding rate from less than 2％ to more than 20％. The refolded Reteplase was purified through two chromatography steps, including lysine-coupled agarose affinity chromatography and then CM-sepharose cation-exchange chomatography. The purity of r-PA was analyzed by Western bolt analysis, and N-terminal amino acid and amino acid composition analyses confirmed the end-product. Reteplase showed higher thrombolytic potency in an animal thrombus model.

• Korean Journal of Food Science and Technology
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• v.18 no.2
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• pp.93-97
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• 1986

Dried barley moodle was made with the addition of gelatinized corn flour as binder by using piston type noodle piston press, in which the temperature was kept below the temperature of protein denaturation. The evacuation of air bubble from the dough strengthened the wet noodle strands and improved the cooking quality of the dry noodle. Although the binder was indispensable, the addition should be less than 20%, because the gelatinized corn flour increased the turbidity of the cooking water. Kneading with 3% solution of soy protein resulted in improvement of the noodle's cooking quality.

• Journal of Ginseng Research
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• v.7 no.1
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• pp.88-93
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• 1983

Studies were carried out to elucidate the protein stabilizing effect of ginseng. Malate dehydrogenase (EC 1.1.1.37) was used as a protein and the rate constant of the enzyme inactivation was determined under the heat denaturation condition. There was an optimum pH for the enzyme stability, the rate constant of the enzyme inactivation was minimum at BH 8.8. The rate constant was increased at lower and higher pH regions than the optimum pH. The inactivation reaction followed the Arrehnius law and the activation energy was measured as 36.8kcal/mole. The reaction rate was not affected by the enzyme concentration and thus it was assumed to be unimolecular first order reaction. The water extract of red ginseng decreased the rate constant of Malate dehydrogenate under heat inactivation condition to stabilize the enzyme activity. Purified ginseng saponin also stabilized the enzyme against heat inactivation.

• Archives of Pharmacal Research
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• v.15 no.2
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• pp.126-129
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• 1992

The critical micelle concentrations (CMCs) of aqueous solutions of a nonionic surfactant, polyoxyl 23 lauryl ether in the presence of various concentration of urea and its derivatives were measured. The CMC of the surfactant increase in proportion to the concentration of the additives, and the CMC-raising activities increased with more and longer alkyl grups substituted in urea. The CMC shift values were successfully correlated with the cloud point shift values and the protein-denaturing activities of the additives, respectively. These results suggest that the micelle formation, clouding of the surfactant and the protein denaturation are a closely related phenomenon, and a common mechanism is operating which might be the hydrophobic interaction.

• Journal of the East Asian Society of Dietary Life
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• v.6 no.2
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• pp.213-219
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• 1996

Addition of reducing agents during extrusion markedly affected physical and chemical properties of wheat flour and gluten extrudates. Expansion at the die was increased for wheat flour and gluten extrudates. Organic materials containing sulfur were evaporated as a flavor from gluten at the die and total sulfur contents were decreased. Physical shape was different for gluten extrudates without reducing agents. It was difficult to form the long strand of gluten extrudate without cooling die. Hydroquinone accelerated cell breakdown and produced more irregular shape of extrudate. However, addition of cysteine decreased the cell breakdown and produced the long strand of gluten extrudates. Chemical reactions of reducing agents such as cysteine and hydroquinone were different for high content (＜80%) of wheat gluten. It was assumed that reducing agents donated hydrogen to inhibit the formation of disulfide crosslinking, decreased the dough strength and produced the broken cell and irregular shape of extrudates. Whereas, cysteine reacted as a binder as well as reducing agent and formed long strands. The evidence of reaction of reducing agents was shown from the fact that non-protein disulfide was increased and protein disulfide was slightly decreased from cysteine added gluten extrudate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.4
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• pp.390-397
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• 1992

This study was carried out to analyze the physicochemical properties of bovine milks, which were heated with LTLT, HTST, UHT pasteurization and UHT sterilization methods and to compare the heat intensity among the heating methods and samples. The mean HMF values per liter milk were measured as 0.66~1.62 $\mu$M (LTLT), 0.9~1.78$\mu$M (HTST), 3.53$\mu$M(UHT pasteurized) and 7.43~8.97$\mu$M (UHT sterilized) in samples, re- sportively. The available Iysine contents per 100ml milk showed 293.2 mg (Raw), 289.2~291.2 mg (LTLT), 298.4~292.4mg (HTST), 272.4~261.6mg (UHT pasteurized) and 279.0mg (UHT sterilized), respectively. The rates of whey protein denaturation were 9.5~11.4% (LTLT), 9.5~17.1% (HTST), 89.3~95% (UHT pas-tsterilized) and 62.7% (UHT sterilized), respectively. The contents of SH groups per g protein were determined as 2.86$\mu$M (Raw) and 2.95~3.15$\mu$M (LTLT), 3.08~3.18$\mu$M (HTST), 3.26~3.42$\mu$M (UHT Pasteurized) and 3. 36$\mu$M (UHT sterilized), respectively, The SS groups Contents per g protein were 28.93$\mu$M (Raw), 25.72~26. 51 $\mu$M (LTLT), 26.93~26.79$\mu$M (HTST), 23.65~23.04 $\mu$M (UHT pasteurized) and 24.69$\mu$M (UHT sterilized), respectively. The ascorbic acid contents per liter milk were measured 6.05mg (Raw), 1.47~1.65mg (LTLT), 2.50~3.85mg (HTST), 2.87~3.69mg (UHT pasteurized) and 4.50mg (UHT sterilized). The changes of some in-dices in milk samples depend on the heating temperature and time ; the HMF values, SH groups, whey protein denaturation rates increased, while the available lysine contents and SS groups decreased in LTLT, HTST, UHT pasteurized and UHT sterilized milks. No remarkable differences were found in heating indicators between LTLT and UHT milks.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.474-481
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• 1996

Since the commercially available rabbit anti-cyclin D3, generated from c-terminal 16 amino acid residues which are common to human and murine cyclin D3, is highly cross-reactive with many other cellular proteins of mouse, a new rabbit polyclonal anti-cyclin D3 has been raised by using murine cyclin D3 protein expressed at a high level in Escherichia coli as the immunogen. To express murine cyclin D3 protein in E. coli, the cyclin D3 cDNA fragment encoding c-terminal 236 amino acid residues obtained by polymerase chain reaction (PCR) was inserted into the NcoI/BamHI site of protein expression vector, pET 3d. Molecular mass of the cyclin D3 overexpressed in the presence of IPTG (Isopropyl $\beta$-D-thiogalactopyranoside) was approximately 26 kDa as calculated from the reading frame on the DNA sequence, and the protein was insoluble and mainly localized in the inclusion bodies that could be easily purified from the other cellular soluble proteins. When renaturation was performed following denaturation of the insoluble cyclin D3 protein in the inclusion bodies using guanidine hydrochloride, 4.4 mg of soluble form of cyclin D3 protein was produced from the transformant cultured in 100ml of LB media under the optimum conditions. Four-hundred micrograms of the soluble form of cyclin D3 protein was used for each immunization of a rabbit. When the antiserum obtained 2 weeks after tertiary immunization was applied to Western blot analysis, it was able to detect 33 kDa cyclin D3 protein in both murine lymphoma cell line BW5147.G.1.4 and human Jurkat T cells at 3,000-fold dilution with higher specificity to murine cyclin D3, demonstrating that the new rabbit polyclonal anti-murine cyclin D3 generated against c-terminal 236 amino acid residues more specifically recognizes murine cyclin D3 protein than does the commercially available rabbit polyclonal antibody raised against c-terminal 16 amino acids residues.