• 한국균학회지
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• 제38권2호
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• pp.152-159
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• 2010

본 연구는 옻나무의 allergy유발성분으로 알려진 urushiol이 장수버섯(Fomitella fraxinea)의 laccase유도에 미치는 영향을 살펴보고 laccase isoenzyme을 분리 정제하여 그 특성을 살펴보았다. 장수버섯의 laccase활성과 균체생산량은 배양 10일째 최대치를 나타내었으며 urushiol첨가에 의해서 효소활성은 2.45배, 균체량은 1.5배 높아졌다. Laccase생산용 배지에서 Cu와 Mn이온을 결핍시켰을 경우 효소활성은 3.8-9.2배 낮아졌으나 균체생산에는 영향이 비교적 적었다. Anion exchange, hydrophobic interaction 및 gel filtration chromatography를 통하여 2종의 laccase isoenzyme(Lac1, Lac2)을 정제하였다. 이 효소는 단량체로 각각 67 kDa(Lac1)과 66 kDa(Lac2)의 분자량을 가지고 있었으며, 등전점은 3.67과 3.81이었다. 두 효소 모두 pH 4.5-5.0, $30-35^{\circ}C$에서 최대 활성을 보였으며, $Fe^{2+}$, $Mg^{2+}$, $Na^+$에 의해서 저해를 받았다. 또한, EDTA와 sodium azide에 의해서도 효소활성이 강하게 저해 받았다.

• 대한약학회:학술대회논문집
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• 대한약학회 2001년도 Proceedings of the Pharmaceutical Society of Korea
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• pp.239-239
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• 2001

• 한국동물학회:학술대회논문집
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• 한국동물학회 1999년도 한국생물과학협회 학술발표대회
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• pp.229.1-229
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• 1999

• Asian Pacific Journal of Cancer Prevention
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• 제14권11호
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• pp.6475-6479
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• 2013

Objectives: Glutathione S-transferase (GST) isoenzymes play important roles in resistance to cell apoptosis and carcinogenesis. We aimed to establish the relationship between GST expression and the prognosis of upper urinary tract urothelial carcinoma (UTT-UC) in Taiwan. Methods: This study retrospectively reviewed 46 patients with pathologically confirmed UUT-UC at Kaohsiung Medical University Hospital. In each patient, expression of GSTT1 and GSTP1 was compared between urothelial carcinoma and normal urothelial cells by Western blotting. Results: GSTP1 expression in the UUT-UC cells was significantly higher than that in normal urothelial cells (1.6 fold, p<0.001). Expression of GSTT1 was significantly associated with the invasiveness of the carcinoma (p=0.006). Conclusions: In UUT-UC, GSTP1 might be a potential tumor marker, whereas high GSTT1 expression could be used as an indicator of cancer progression. This study is the first to demonstrate potential applications of different GST isoenzymes for biomolecular analysis of UUT-UCs in Taiwan.

• BMB Reports
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• 제37권2호
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• pp.199-205
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• 2004

The six lumbrokinase fractions (F1 to F6) with fibrinolytic activities were purified from earthworm Lumbricus rubellus lysates using the procedures of autolysis, ammonium sulfate fractionation, and column chromatography. The proteolytic activities on the casein substrate of the six iso-enzymes ranged from 11.3 to 167.5 unit/mg with the rank activity orders of F2 > F1 > F5 > F6 > F3 > F4. The fibrinolytic activities of the six fractions on the fibrin plates ranged from 20.8 to 207.2 unit/mg with rank orders of F6 > F2 > F5 > F3 > F1 > F4. The molecular weights of each iso-enzyme, as estimated by SDS-PAGE, were 24.6 (F1), 26.8 (F2), 28.2 (F3), 25.4 (F4), 33.1 (F5), and 33.0 kDa (F6), respectively. The plasminogen was activated into plasmin by the enzymes. The optimal temperature of the six iso-enzymes was $50^{\circ}C$, and the optimal pH ranged from pH 4-12. The four iso-enzymes (F1-F4) were completely inhibited by PMSF. The two enzymes (F5 and F6) were completely inhibited by aprotinin, TLCK, TPCK, SBTI, LBTI, and leupeptin. The N-terminal amino acid (aa) sequences of the first 20 to 22 residues of each fraction had high homology. All six isoenzymes had identical aa residues 2-3 and 13-15. The N-terminal 21-22 aa sequences of the F2, F3, and F4 isoenzymes were almost the same. The N-terminal aa sequences of F5 and F6 were identical.

• 한국식품과학회지
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• 제19권5호
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• pp.397-402
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• 1987

황산암모늄분획 침전, 이온교환컬럼 크로마토그래프를 이용하여 감자로부터 2개의 Lipoxygenase isozyme(F-I 및 F-II)을 분리정제하고 각각의 isozyme에 대하여 열불활성화 실험을 행하였다. 분리된 isozyme은 polyacrylamide gel 전기 영동상에서 단일밴드를 보였으며 두 isozyme의 최적 pH는 $5.5{\sim}6.0$으로 비슷하였다. 열불활성화 온동 범위인 $50{\sim}60^{\circ}C$에서 F-I 및 F-II의 $D_{65}$값은 각각 13.3min 및 4.3min이었으며 Z 값은 $11.8^{\circ}C$ 및 $10.3^{\circ}C$ 이었다. 또한 각 isozyme의 열역학적인 상수를 절대반응속도식에 따라 구하였다.

• International Journal of Industrial Entomology and Biomaterials
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• 제18권2호
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• pp.131-134
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• 2009

The purpose of this study was to establish whether there are differences in the productivity of the same silkworm(Bombyx mori L.) parthenoclones, obtained by two different methods-thermal and combined, as well as to study their genotype structure by several enzyme loci. It was established that all individuals of parthenoclones Joana, Joana(${\downarrow}{\uparrow}$), Pohi and Pohi(${\downarrow}{\uparrow}$), are homozygous by the studied esterase and phosphoglucomutase loci, which substantiated the clones' genetic stability. By comparative analysis of some biological and technological properties, it was found that parthenoclone Pohi(${\downarrow}{\uparrow}$) obtained by low-high temperature activation is characterized by higher values of these properties as compared to parthenoclone Pohi obtained by thermal parthenogenesis. Comparing the two methods of inducing ameiotic parthenogenetic development, we would recommend that parthenoclone Joana is sustained by thermal parthenogenesis, and parthenoclone Pohi-by the combined method (low-high temperature).

• Journal of Nutrition and Health
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• 제26권8호
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• pp.998-1005
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• 1993

This study was attempted to investigate the effects of enzymatic modification of milk protein with Meju protease on its acid clotting and digestibility. The proteases used in this study were isolated from Meju(fermented soybeans) and had specific acticity of 250 units/mg protein at pH 7.0. These proteases were found to be at least 3 different isoenzymes of different pH optima(pH 4.0, 6.0, 10.0). The optimum temperature was 5$0^{\circ}C$. Hydrolyzed skim milk showed 30.5% degree of hydrolysis for 1 hr. and 36.4% degree of hydrolysis for 3.5 hrs. of protease treatment at pH 7.0. Upon acidification to pH 4.0, skim milk produced large and dense coagulum, but the coagulum was getting smaller by protease treatment. Generally, digestability of skim milk at pH 4.0 was lower than pH 2.0. At pH 4.0, native skim milk and control group had problem with hydrolysis of skim milk protein. Among protease treated groups, 1 hour treated skim milk was most effectively hyrolyzed at pH 4.0.

• Journal of Ginseng Research
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• 제37권1호
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• pp.117-123
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• 2013

Polyphenol oxidase (PPO) was purified from fresh ginseng roots using acetone precipitation, carboxymethyl (CM)-Sepharose chromatography, and phenyl-Sepharose chromatography. Two isoenzymes (PPO 1 and PPO 2) were separated using an ion-exchange column with CM-Sepharose. PPO 1 was purified up to 13.2-fold with a 22.6% yield. PPO 2 bound to CM-Sepharose, eluted with NaCl, and was purified up to 22.5-fold with a 17.4% yield. PPO 2 was further chromatographed on phenyl-Sepharose. The molecular weight of the purified PPO 2 from fresh ginseng was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was about 40 kDa. The optimum temperature and pH were $20^{\circ}C$ and 7.0, respectively, using catechol as a substrate. Pyrogallol showed the highest substrate specificity. The effect of a PPO inhibitor showed that its activity increased slightly in the presence of a low concentration of citric acid. High concentrations of acidic compounds and sulfite agents significantly inhibited purified ginseng PPO 2.

• International Journal of Industrial Entomology and Biomaterials
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• 제15권2호
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• pp.145-155
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• 2007

Mulberry (Morus spp.) is an economically important tree crop being cultivated in India, China and other sericulturally important countries for its foliage to feed the silk producing insect Bombyx mori L. Genetic improvements of mulberry lag behind to the same in many other economically less important crops due to the complexity of its genetics, the breeding behavior, and the lack of basic information on factors governing important agronomic traits. In this review, the general usage and advantages of different molecular markers including isoenzymes, RFLPs, RAPDs, ISSRs, SSRs, AFLPs and SNPs are described to enlighten their applicability in mulberry genetic improvement programs. Application of DNA markers in germplasm characterization, construction of genetic linkage maps, QTL identification and in marker-assisted selection was also described along with its present status and future prospects.