• Biomedical Science Letters
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• v.11 no.3
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• pp.301-305
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• 2005

MR spectroscopy of intracellularly located $^{133}Cs$ has been used to monitor the uptake of Gd-EOB-DTPA by the isolated rat liver. As shown by ${31}P$ spectroscopy, accumulation of $^{133}Cs$ ions in hepatocytes does not produce detectable effects on the metabolism. The hepatic internalization of Gd-EOB-DTPA was followed by the paramagnetic relaxation enhancement of the intracellular $^{133}Cs$ ions, and confirmed by parallel quantitations of Gd and Cs run by inductively coupled plasma analysis of liver samples and aliquots of perfusate. Two peaks are observed at -22.0 and -23.5 ppm, with respect to the line of the external reference arbitarily set to 0 ppm. Upon rinsing of the extracellular compartment with regular K-H free of CsCl, the high-field resonance disappears within 20min. The intracellular concentration was confirmed by ICP, which gives a $Cs^+$ content of $22.0\pm3.5mM$. The relaxation data significantly underestimate the Gd content, suggesting a potential compartmentation of $Cs^+$ and the contrast agent.

• Proceedings of the KSME Conference
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• 2008.11a
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• pp.1455-1457
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• 2008

Cell adhesion is a coordinated process involving initial binding of integrin receptors to extracellular matrix (ECM), recruitment of adhesion proteins, and focal adhesion assembly. The formation of mechanically stable focal adhesion assembly of cells within surrounding ECM is a key parameter to direct numerous cellular functions including cell migration, differentiation, and apotosis. With current cell adhesion assays, it is difficult to understand contributions of each coordinated event on evolution of cell adhesion strengthening since cells spontaneously spread upon their adhesion to the substrate, thus remodeling their cytoskeletal structure. In this presentation, novel approaches for analysis of cell adhesion strengthening process based on the combination of mechanical device, micro-patterned substrates, and molecular biological techniques will be discussed.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.861-869
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• 1999

An extracellular protease was purified to homogeneity from the culture supernatant of psychrotrophic bacteria Bacillus sp. JH 108 using procedures including ammonium sulfate fractionation, anion exchange chromatography, gel filtration chromatography, and cation exchange chromatography. The enzyme exhibited a molecular weight of 36 kDa, an optimum pH of 8 to 9, and optimum temperature of $60^{\circ}C$. The enzyme preferentially hydrolyzed leucine at the N-terminus of peptides and thus can be classified as an aminopeptidase. It was strongly inhibited by metal chelating agents such as EDTA and l, l0-phenanthroline. The activity lost by EDTA was restored with $Zn^{2+}{\;}or{\;}Co^{2+}$. These divalent cations also stimulated the native enzyme. This suggests that the enzyme is a metalloprotease acting as a leucine aminopeptidase.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1979.10a
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• pp.248.1-248
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• 1979

Sixteen temperature-sensitive mutants of Autographa californica nuclear polyhedrosis virus were isolated. Several interesting phenotypes were observed. A large proportion of the mutants were un-able to form polyhedral occlusion bodies at the nonpermissive temperature (32.5C). At 32.5C, one mutant formed plaques in which the cells lacked polyhedra. Another mutant type was defective in the production of progeny extracellular nonoccluded virus and produced a plaque consisting of only a single cell containing polyhedra at 32.5C. One mutant was defective in plaque formation, progeny nonocluded virus formation, and polyhedra formation at 32.5C. Several mutants produced nonocluded virus but failed to produce plaques or polyhedra at 32.5C. Other phenotypes were also distinguished. Complementation analyses, performed by either measuring the increase in extracellular non-ocludedvirus formation or by oberving polyhedra formation in mixed infections at 32.5C, indicated the presence of 15 complementation groups. A high frequency of recombination was observed. Four of the mutants were found to be host dependent in their temperature sensitivity for polyhedra formation.

• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.313-316
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• 2002

Effect of Pluronic F-68, a nonionic surfactant, on the extracellular production of hGM-CSF in transgenic Nicotiαna tabacum cell suspension culture was investigated. The addition of 5 g/L Pluronic F-68 did not affect the cell growth but increased the extracellular production of hGM-CSF by two-fold. This may be due to the enhanced permeability of the cell membrane by the interaction between the Pluronic F-68 and the cell membrane.

• KSBB Journal
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• v.5 no.3
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• pp.293-298
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• 1990

Alpha-interferon was produced by using recombinant Escherichia coli strains, which carry cloned alpha-interferon gene in plasmid vectors, pIF-III-B and pIF-III-C. With the aid of signal sequence of E. coli lipoprotein, which is placed right in front of the upstream of the cloned alpha-interferon gene of the plasmids, about 50% of alpha-interferon produced was excreted or secreted. Meanwhile, there was no extracellular production of alpha-interferon from the recombinant strain carrying the plasmid Hif-2h that lacks the signal sequence of lipoprotein.

• Journal of Microbiology and Biotechnology
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• v.3 no.4
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• pp.244-251
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• 1993

A novel system has been developed to produce ${\delta}-aminolevulinic$ acid (ALA) using the intact cells of late logarithmic phase of Rhodocyclus gelatinosus KUP-74. The system was shown optimum yield of extracellular ALA under a condition of anaerobic light irradiation (4 Klux) at $30^{\circ}C$ with no variation in cell mass. The rate of extracellular ALA formation was stimulated by low doses of either $C_4\;or\;C_5$ ALA biosynthetic precursors, where 5 mM ($C_4) and 3 mM ($C_5) of each precursors were appeared to generate the maximum rates of 3.3 and 4.0 nmoles of ALA per 0.35 mg cells per hr, respectively. Half-life of the system was 10 hr in a sense of an ability of portage transport of L-glutamate, and sequential dose of this compound was resulted in promising recovery of the ALA.

• Archives of Plastic Surgery
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• v.40 no.5
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• pp.517-521
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• 2013

Background Diabetes is characterized by chronic hyperglycemia, which can increase reactive oxygen species (ROS) production by the mitochondrial electron transport chain. The formation of ROS induces oxidative stress and activates oxidative damage-inducing genes in cells. No research has been published on oxidative damage-related extracellular superoxide dismutase (EC-SOD) protein levels in human diabetic skin. We investigated the expression of EC-SOD in diabetic skin compared with normal skin tissue in vivo. Methods The expression of EC-SOD protein was evaluated by western blotting in 6 diabetic skin tissue samples and 6 normal skin samples. Immunohistochemical staining was also carried out to confirm the EC-SOD expression level in the 6 diabetic skin tissue samples. Results The western blotting showed significantly lower EC-SOD protein expression in the diabetic skin tissue than in the normal tissue. Immunohistochemical examination of EC-SOD protein expression supported the western blotting analysis. Conclusions Diabetic skin tissues express a relatively small amount of EC-SOD protein and may not be protected against oxidative stress. We believe that EC-SOD is related to the altered metabolic state in diabetic skin, which elevates ROS production.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1998.11a
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• pp.161-161
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• 1998

To achieve the aim of this investigation, the extracellular protease was isolated from bacteria BAC-4, a strain was cultivated in the medium for the production of penicillin acilase in a period of 32 hours. The enzyme was first purified by aceton precipitation method, followed by ion exchange chromatography on DEAE-sephacel column. The highest specific activity of the aceton fraction was found to be 2.19 unit per mg, with degree of purification of 13 times. Further purification of the enzyme on DEAE -sephacel had a specific activity of 58.6 unit per mg and degree of purification of 344 times compared to its crude extract. The optimum pH of the enzyme was 8.4, and the potimum temparature was 37$^{\circ}C$. The K$\_$M/ and $V_{max}$ calculated at experiment conditions were found to be 0.66%(W/V) and 3.61 unit per mL respectively.

• 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.