• ALGAE
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• v.22 no.2
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• pp.131-139
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• 2007

The expression of genes responding to cold stress in a freshwater alga, Spirogyra varians, was studied by using differential expression gene (DEG) method. A gene strongly up-regulated in 4°C was isolated and designated as SVCR2 (Spirogyra varians cold regulated) gene. The cDNA encoding SVCR2 was cloned using λZAP cDNA library of Spirogyra varians. The deduced amino acid had a sequence similarity with trans-membrane protein in Arabidopsis thaliana (Q9M2D2, 52.7%). Northern blot analysis demonstrated that transcript level of SVCR2 increased about 10 fold under low temperature (4°C), compared with that cultured at warm (20°C) conditions. The expression of SVCR2 was also affected by light conditions. When the plants were exposed to high light (HL) (1200 μmol photon m–2 s–1), the expression of SVCR2 began within 2 hrs. This gene expression lasted for 4 hrs and decreased afterwards. Under the blue light (470 nm) condition, the expression of this gene was induced in same way as HL treatment, even under less than 100 μmol photon m–2 s–1. But red light (650 nm) and UV-A irradiation did not affect the expression of SVCR2.

• Electrical & Electronic Materials
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• v.8 no.1
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• pp.71-76
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• 1995

The thermal oxidation of Ge$_{0.2}$Si$_{0.8}$ in wet ambient has been investigated by Rutherford Backscattering Spectrometry(RBS). A uniform Ge$_{0.2}$Si$_{0.8}$O$_{2}$ oxide is formed at temperatures below 650.deg. C for polycrystalline and below 700.deg. C for single crystalline substrates. At higher temperatures Ge becomes depleted from the oxide and finally SiO$_{2}$ oxide is formed with Ge piled-ub behind it. The transition between the different oxide types depends also on the crystallinity of Ge$_{0.2}$Si$_{0.8}$. When a uniform Ge$_{0.2}$Si$_{0}$8/O$_{2}$ oxide grows, its thickness is proportional to the square root of the oxidation time, which suggests that the rate noting process is the diffusive transport of oxidant across the oxide. It is believed the oxidation is controlled by the competition between the diffusion of Ge or Si in Ge$_{0.2}$Si$_{0.8}$ and the movement of oxidation front.t.oxidation front.t.

• Korean Journal of Microbiology
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• v.29 no.4
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• pp.230-237
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• 1991

Citrate synthase 1 (mitochondrial) and citrate synthase 2 (nonmitochondrial) were purified from Saccharomyces cerevisiae. The physical and enzymatic characteristics of citrate synthase 2 were ananlyzed in comparison with citrate synthase 1. Both isoenzymes were shown to be dimeric proteins of identical subunits, and the molecular weights of the subunits were estimated to be 48.3kDa for citrate synthase 1 and 47.0kDa for citrate synthase 2, respectively. The optimal pH value for enzyme activity was pH 7.5 for both isoenzymes. However, the optimal temperature for the activity was strikingly different; while the activity of citrate synthase 1 reached its peak at 65.deg.C, that of citrate synthase 2 was maximal at 40.deg.C. Citrate synthase 2 showed much lower thermal and pH stability than citrate synthase 1. In addition, citrate synthase 2 was affected much more by the metal ions such as $Zn^{2+}$ , $Mn^{2+ , and $Co^{2+} than citrate synthase 1. Among the several possible regulatory metabolites tested, ATP showed the strongest inhibitory effect on both enzymes. ADP and NADH were found to have greater effect on citrate synthase 2 than on citrate synthase 1. Kinetic analysis revealed that citrate synthase 2 has approximately 7- and 3.5-fold lower affinity to acetyl CoA and to oxaloacetate, respectively, than citrate synthase 1.

• Transactions of the Korean Society of Mechanical Engineers
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• v.7 no.4
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• pp.425-433
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• 1983

Fatigue tests by axial loading (R=0.1) were carried out to investigate fatigue crack growth properties of small surface cracks in mild steel at room temperature, 250.deg. C and 400.deg. C, by using flat specimens with a small artificial pit. All the data of the fatigue crack growth rate obtained in the present tests are determined as a function of the stress intensity factor range, so that the applicability of liner fracture mechanics to the fatigue crack growth of surface cracks at elevated temperatures is investigated and discussed in comparison with the data of type 304 stainless steel at room temperature and elevated temperature. The obtained results are as follows: 1) Relations of both surface fatigue crack length and its depth to cycle ratio fall within a narrow scatter band in spite of different stress levels. 2) The .DELTA. .sigma. .root. .pi. a-da/dN relation of surface fatigue crack growth at room temperature is independent of the stress level and can be plotted as a straight line at log-log diagram, but the relation at 400.deg. C depends partly on the stress level. 3) Relations of the fatigue crack growth into depth d(2b)/dN and is stress intensity factor range .DELTA. $K_{I}$, accounted for the aspect ratio variation, fall within a narrow scatter band for wide range of the applied stress levels. And .DELTA. $K_{I}$E-d(2b)/dN relations of mild steel at different stress level coincide relatively well with the data of type 304 stainless steel. 4) The value of aspect ratio obtained by a beach mark method and a temper coloring method approaches about 0.9 in common with crack growth and it is independent of stress level and temperatures. 5) The equi-crack length curve is parallel to S-N$_{f}$ curve at elevated temperatures.s.s.s.

• Korean Journal of Microbiology
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• v.14 no.2
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• pp.65-74
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• 1976

Atternaria sp. was isolated from soil and crude cellulases were prepared from wheat bran culture of the fungus. The activities of the crude enzyme were studied on five different subvstrates and some phsical properties were also examined, crude enzymes were purified by column chromatography on DEAE Sephadex and Sephadex, Isozymes were separated some of which were active specifically on DEAE cellulose and some were primarily active on cellulose and CM-cellulose. The optimal points of pH and temperature for the crude enzyme were varied depending on the substrates ; On cellulose they were at pH 6.0 and 40.deg.C, on CM-cellulose at pH's 4.0 and 6.0 and 60.deg.C, and on DEAW-cellulose at pH 5.0 and 50.deg.C. Two active fractions, F-1 and F-II on Na-CMC was used as substrate the Km values of crude enzyme, F-I and F-II were calculated to be $4{\times}10^{-5}$ , 1.1 * 10$^{-4}$ , and $1.25{\times}10^{-4}mN$ resepctively. The Ki value of $Cu^{++}$ for crude enzyme was$4{\times}^{-4}mN$ , while that of $Nm^{++}$ while in the same concentration of $Mn^{++}$ it reached to 91%. Some 57% activity of F-1 was inhibited in s mN $Cu^{++}$, whereas it was inhibited as much as 81% in the same concentration above the concentration of 0.3 mM with tis activity reaching up to 137% in 2 mM. On the other hand the F-11 was inhibited by the presence of M $n^{++}$ and some 67% activity was inhibited at 2mM.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2008.06a
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• pp.151-151
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• 2008

갈륨-질화물(GaN) 기반의 고속전자이동도 트랜지스터(high electron mobility transistor, HEMT)는 마이크로파 또는 밀리미터파 등과 같은 고주파 대역의 통신시스템에 널리 사용되는 전자소자로 각광받고 있다. GaN HEMT는 AlGaN/GaN 또는 AlGaN/InGaN/GaN 등과 같은 이종접합구조(heterostructure)로부터 발생하는 이차원 전자가스(two-dimensional electron gas, 2DEG) 채널을 이용하여 캐리어 구속효과(carrier confinement) 및 이동도의 향상이 가능하다. 또한 높은 2DEG 채널의 면밀도(sheet concentration) 와 전자의 포화 속도(saturation velocity)를 바탕으로 고출력 동작이 가능하여 차세대 이동통신용 전력 증폭기로 주목받고 있다. 그러나 이론적으로 우수한 특성과 달리, 실제 소자에서는 epi 성장시의 결함이나 전위, 표면 상태에 따른 2DEG 감소 등의 영향으로 이론보다 높은 누설 전류와 낮은 항복 전압 특성을 가진다. 특히, 기존의 GaN HEMT 구조에서는 Drain-Side Gate Edge에서의 전계 집중이 항복 전압 특성에 미치는 영향이 크다. 본 논문에서는 이러한 문제를 해결하기 위해 Trapezoidal Gate구조를 이용하여 Drain 방향의 Gate Edge가 완만히 변하는 구조를 제안하였다. 이를 위해 $ATLAS^{TM}$ 전산모사 프로그램을 이용하여 Trapezoidal Gate 구조를 구현하여 형태에 따른 전류-전압 특성 및 소자의 스위칭 특성 및 Gate 아래 채널층에 형성되는 Electric Field의 분산을 조사하고, 이를 바탕으로 고속 동작 및 높은 항복 전압을 갖는 AlGaN/GaN HEMT의 최적화된 구조를 제안하였다. 새로운 구조의 Gate를 적용한 AlGaN/GaN HEMT는 Gate edge에서의 전계를 분산시켜 피크 값이 감소되는 것을 확인하였다.

• Electrical & Electronic Materials
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• v.8 no.3
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• pp.278-284
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• 1995

Thin fihn SnO$_{2}$ Gas Sensor was fabricated by electron-beam evaporation system and the target made by general firing method for the purpose of detecting gas components in air, especially methane gas. SnO$_{2}$ thin film was prepared on the polished alumina substrate which Pt interdigital electrode was precoated. The effects of annealing temperature and substrate temperature on the structural properties of SnO$_{2}$ thin film on glass were investigated using the X-ray diffraction. The good crystalline structure is formed when substrate temperature is 150[.deg. C] and annealing condition is 550[.deg. C], 1[hour]. And the sensing properties at various thickness of the SnO$_{2}$ thin film and the effects of PdCI$_{2}$ addition were also investigated. The good result is showed when the thickness is below 1000[.angs.] and the quantity of PdCI$_{2}$ addition is 4[wt%]. The thickness of SnO$_{2}$ thin film was measured by .alpha.-step and Elliopsometer.

• Electrical & Electronic Materials
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• v.10 no.2
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• pp.126-133
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• 1997

In order to apply for the gas sensing layer and the piezoelectric thin film devices, we studied the effects of magnetron sputtering conditions and annealing temperature on the electrical and structual characteristics of the ZnO thin film. The optimal deposition conditions, in order to obtain a c axis of the ZnO (002) phase thin film which is perpendicular to SiO$_{2}$/Si substrate, were like these ; substrate temperature 150.deg. C, chamber pressure 2 mtorr, R.F. power 300 watts, gas flow ratio 0.4[O$_{2}$(Ar + $O_{2}$)]. When the ZnO thin film was annealed in 600.deg. C, $O_{2}$ gas ambient for 1 hr, the resistivity was 2.6 x 10$^{2}$.ohm.cm and the grain size of ZnO thin film was less than 1 .mu.m. So the ZnO thin film acquired from above conditions can apply for the gas sensing layer which require a c axis perpendicular to the substrate surface.

• Electrical & Electronic Materials
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• v.10 no.10
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• pp.1056-1062
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• 1997

• Korean Journal of Microbiology
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• v.31 no.1
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• pp.54-62
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• 1993

Intracellular adenosine deaminase (ADA) from Aspergillus oryzae was purified using ammonium sulfate fractionation, a DEAE-Sephadex A-50 anion exchange chromatography, an ultrafiltration using a PM 10 membrane and two times of Sephadex G-100 gel filtration chromatography. The enzyme was purified 151 fold with a 9% recovery. Purified enzyme gave a single protein band with a molecular weight of 105,000 delton. The enzyme was reasonably stable. The enzyme activity was kept even after 1 hr incubation at 55.deg.C, but decreased significantly at 60.deg.C. The pH optimum was found to be from 6.5 to 7.5. Among tested compounds, the substrate activity was found with adenosine, adenine arainofuranoside, formymcin A, 2'-deoxyadenosine, 3'-deoxyadenosine, 2', 3'-isopropylidene adenosine, 2,6-diaminopurine deoxyriboside, .betha.-nicotinamide adenine dinucleotide (reduced form), 6-chloropurine riboside, 2'-adenine monophosphate (AMP), 3'-AMP and 5'-AMP. The values of Km of adenosine and 2'-deoxyadenosine were calculated to be 500 and .$710\mu$m, respectively. ADA was sensitivite to $Zn^{2+}$, $^Cu{2+}$ and $Fe^{3+}$, p-chloromercuribenzoate and mersalyl acid inactivated the enzyme. The activity of enzyme was not changed when ADA was incubated with dithiothreititol, 2-mercaptoethanol, N-ethylmaleimide, iodoacetic acid and iodoacetamide.