• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.34 no.2
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• pp.151-156
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• 2008

Different kinds of forces can be applied to the biological tissue. The analysis of the applied force is highly important to explain the mechanism of cellular response. In this study, the applied force to the collagen gel was analyzed by the finite elements analysis. The model received two different kinds of static force (compression and tension). The force range was 50g to 400g. In results, von Mises stress was concentrated in the peripheral region in the compression model. It was concentrated in the central area in the tension model. However, the compressive force was high in the peripheral area of the compression model and the tensional force was also high in the same area of the tension model. In conclusion, the applied force could be different to the region and it should be considered in the experiment to analyze the effects of the mechanical force on the cells.

• Fisheries and Aquatic Sciences
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• v.25 no.1
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• pp.31-39
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• 2022

To clarify the factors influencing the physical properties of fish after heat treatments, we investigated changes in the properties of proteins in the dorsal ordinary and dark muscle of yellowtail (Seriola quinqueradiata) heated under different conditions commonly used for the purposes of food hygiene. High-temperature/short-time heating (85℃ for 90 s and 75℃ for 60 s) affected the protein solubility more than low-temperature/long-time heating (63℃ for 30 min). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and differential scanning calorimetry showed that low-temperature/long-time heating reduced the degree of actin denaturation in fish compared with that by other heating conditions. In addition, collagen solubility was enhanced with low-temperature/long-time heating. Therefore, these results suggest that differences in the degree of actin and collagen denaturation are responsible for the enhanced meat tenderness and diminished meat shrinkage, resulting from low-temperature/long-time heating.

• Journal of Pharmaceutical Investigation
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• v.31 no.2
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• pp.101-106
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• 2001

Alginate-chitosan (anion-cationic polymeric complex) was prepared to control the release rate of silver sulfadiazine (AgSD). Na-alginate (2%) solution containing AgSD was gelled in $CaCl_2$ solution. The gel beads formed were immediately encapsulated with chitosan (CS). The gel matrix and membrane were then reinforced with chondroitin-6-sulfate (Ch6S). Release rate of AgSD from the gel matrix was investigated by placing alginate beads in the sac of cellulose membrane simmered in HEPES-buffer solution. The concentration of AgSD released was analyzed by UV at 264 nm. Incorporation capacity of AgSD in Ca-alginate gel was more than 90%. Alginate-Ch6S-CS could control the release rate of AgSD. The amount of AgSD release was dependent on the AgSD loading dose. Incorporation of tripolyphosphate (polyanionic crosslinker) onto the alginate-Ch6S-CS bead increased the release rate of AgSD. Collagen-coating had no influence on the AgSD release rate. Alginate-Ch6S-CS beads with a sufficiently high AgSD encapsulation were capable of controlling the release of the drug over 10 days. In summary, alginate-Ch6S-CS beads could be used as a sustained delivery for AgSD and provide local targeting with low silver toxicity and patient discomfort.

• BMB Reports
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• v.32 no.5
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• pp.445-450
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• 1999

We purified and characterized a bovine pregnancy-associated protein in pregnant cow urine using two-dimensional gel electrophoresis. Urine from cows was collected according to their status of pregnancy and non-pregnancy. Proteins in the cow urine were fractionated with 50% ammonium sulfate prior to two-dimensional gel electrophoresis. Proteins separated on the gels were compared in terms of expression level and new expression by molecular mass and isoelectric point. We localized two pregnancy-associated protein spots on the gels at molecular masses of 24 kDa and 20 kDa and isoelectric points of 5.5 and 5.7, respectively. Likewise, two non-pregnancy specific proteins were localized at 27 kDa and 28 kDa with isoelectric points of 5.7 and 5.9, respectively. To rule out the possibility that environmental or genetic factors might influence the expression of the proteins, we demonstrated the pregnancy-associated expression of the proteins in two-dimensional gels with pregnant urine taken from cows raised in a different institute. The pregnancy-associated protein with molecular mass of 20 kDa and isoelectric point of 5.7, namely spot 2, was microsequenced and found to be highly homologous to the bovine collagen alpha 1 chain.

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.260-265
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• 1998

Angiogenic activity of Aloe vera gel was investigated by in vitro assay. We obtained the most active fraction from dichloromethane extract of Aloe vera gel by partitioning between hexane and 90% aqueous methanol. The most active fraction (F3) increased the proliferation of calf pulmonary artery endothelial (CPAE) cells. In addition, F3 fraction induced CPAE cells to invade type I collagen gel and form capillary-like tube through in vitro angiogenesis assay, and increased the invasion of CPAE cells into matrigel through in vitro invasion assay. Furthermore, the effect on the MRNA expression of proteolytic enzymes which are key participants in the regulation of extracellular matrix degradation was investigated by northern blot analysis. F3 fraction enhanced mRNA expression of urokinase-type plasminogen activator (u-PA), matrix metalloproteinase-2 (MMP-2), and membrane-type MMP (MT-MMP) in CPAE cells whereas the expression of plasminogen activator inhibitory (PAl-1) mRNA was not changed.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.5
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• pp.588-593
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• 2006

This study was intended to observe possibility of which radiation technique can be used for oligopeptide production from pigskin collagen to reduce environmental pollution in processing and simplify the processing steps. Raw pigskin was ground using chopper, and then defatted in acetone cooled at $-20^{\circ}C$ freezer. Defatted dried pigskin was irradiated at 20, 40, 60, 100, 150, 200, 250, and 300 kGy using Co-60 gamma rays irradiator. With irradiation doses, the amount of soluble proteins increased, and the viscosity and turbidity of soluble proteins decreased, which could be clue of that irradiation degrade high molecular proteins directly. pH of soluble proteins from defatted pigskin increased in the sample above 150 kGy, and low molecular weight components (below 24 kDa) in SDS-PAGE increased. From gel permeation chromatography of the hydrolysates of pigskin irradiated at 300 kGy showed the major peak of 9,000, 8,200, 860, and 170 Da.

• 대한생식의학회:학술대회논문집
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• 2003.12a
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• pp.109-110
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• 2003

• Proceedings of the KSLP Conference
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• 1998.11a
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• pp.195-195
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• 1998

성문부폐쇄부전(glottic insufficiency)를 수술적으로 치료하기 위한 노력은 여러 형태(silicone, hydrogen gel, teflon, etc.)의 성대이물주입술, 갑상성형술등 다양하게 시도되어 왔다. 그러나, 이러한 노력에도 불구하고 성문부폐쇄부전은 여전히 해결하기 어려운 문제로 남아있다. 여기에 1995년 Ford 등은 성문부폐쇄부전에 이은 음성장애치료의 새로운 접근방법으로 자가 콜라겐주입술(autologous collagen injection)을 소개하였다. (중략)

• Korean Journal of Microbiology
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• v.29 no.6
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• pp.345-352
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• 1991

A serine proteinase of molecular weight 60 kd was purified from culture supernatant of P. aeruginosa using DEAE-Trisacryl M ion-exchange and AcA 54 gel filtration column chromatography, and the properties of serine proteinase were characterized. By means of SDS-polyacrylamide gel electrophoresis, the molecular weight of the enzyme was 55 kd. The optimal pH for the activity of purified enzyme was 7.5. The activity of the purified enzyme was completely inhibited by Di-isopropylfluorophosphate(DFP) and N-.alpha.-p-tosyl-L-lysine choloromethyl detone(TLCK) but not by other proteinase inhibitors such as E-64, pepstatin A, 1, 10-phenanthroline. The purified enzyme was capable of degrading type I and type IV collagen. Antisera obtained from hymans infected with Pseudomonas aeruginosa reacted to the purified serine proteinase in immunoblots. These results indicate that the purified enzyme is trypsin-like serine proteinase and this enzyme of P. aeruginosa may play an important role in tissue damage as a spreading factor and may be useful for serodiagnosis of Pseudomonas infections.

• Journal of Life Science
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• v.13 no.3
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• pp.308-313
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• 2003

The collagenase gene from Vibrio parahaemolyticus 04 was subcloned into an expression vector pET-29b. The recombinant collagenase was expressed in Escherichia coli BL2l(DE3) and partially purified by Hi-Trap affinity and Sephacryl S-100 size exclusion chromatographies. The recombinant enzyme was purified by 43.7-fold and the yield was 73%. SDS-PAGE revealed that the molecular weight of the enzyme was approximately 35 kDa. Substrate specificity study of the enzyme displayed that the enzyme showed the highest activity with the type I collagen and the synthetic peptide, Z-GPGGPA, indicating that the enzyme was indeed a collagenase. The enzyme showed broad pH optimum around pH 6-12 and was stable between pH 5.5 and 11.5. The optimum temperature for the type I collagen degradation was $35^{\circ}C$. The thermostability measurement of the enzyme indicated that the enzyme was stable up to $55^{\circ}C$, but the activity was diminished quickly above $60^{\circ}C.$