• Journal of applied mathematics & informatics
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• v.32 no.1_2
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• pp.113-128
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• 2014

Consider a class of p(x)-Kirchhoff type equations of the form $$\left\{-M\left({\int}_{\Omega}\;\frac{1}{p(x)}{\mid}{\nabla}u{\mid}^{p(x)}\;dx\right)\;div\;({\mid}{\nabla}u{\mid}^{p(x)-2}{\nabla}u)={\lambda}V(x){\mid}u{\mid}^{q(x)-2}u\;in\;{\Omega},\\u=0\;on\;{\partial}{\Omega},$$ where p(x), $q(x){\in}C({\bar{\Omega}})$ with 1 < $p^-\;:=inf_{\Omega}\;p(x){\leq}p^+\;:=sup_{\Omega}p(x)$ < N, $M:{\mathbb{R}}^+{\rightarrow}{\mathbb{R}}^+$ is a continuous function that may be degenerate at zero, ${\lambda}$ is a positive parameter. Using variational method, we obtain some existence and multiplicity results for such problem in two cases when the weight function V (x) may change sign or not.

• Animal cells and systems
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• v.5 no.2
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• pp.145-151
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• 2001

p62 is a phosphotyrosine-independent ligand of the SH2 domain of $p56^{Ick}$, a T-cell specific Src family tyrosine kinase. Recently p62 has been shown to interact with a number of proteins, such as $PKC\varsigma$ and ubiquitin, and implicated in important cellular functions such as cell proliferation. Since the two p62 interacting proteins, $p56^{Ick}$ and $PKC\varsigma$, have been reported to play roles in cell death, 1 have addressed the potential role of p62 during apoptosis in Jurkat cells in this study. Herein 1 show that p62 was specifically cleaved into two peptides by a caspase-3-like activity during Fas-receptor mediated apoptosis in Jurkat cells. This cleavage generated two fragments with molecular weights of about 35 kDa that differed in subcellular localizations. The N-terminal cleaved fragment was present in the detergent-insoluble fraction whereas the C-terminal fragment was found in the detergent-soluble fraction. In addition, the C-terminal fragment appeared to be subjected to further degradation as apoptosis prolonged. Moreover, overexpression of p62 in Jurkat cells attenuated the Fas receptor mediated apoptosis, suggesting that p62 is involved in apoptotic signal transduction pathway in lymphocytes.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.10
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• pp.1501-1509
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• 2003

The simultaneous addition of xylanase (5,600 EXU/kg) and phytase (500 FTU/kg) feed enzymes to wheat-based broiler diets was investigated. Starter, grower and finisher diets, with three tiers of nutrient specifications, were fed to 1,440 broiler chicks kept on deep litter from 1-42 days post-hatch, without and with xylanase plus phytase, to determine the effects of diet type and enzyme supplementation on growth performance. The nutrient specifications of type A diets were standard; energy density and protein/amino acid levels were reduced on a least-cost basis to formulate type B diets and further reduced to type C diets. Phosphorus (P) and calcium (Ca) levels were adjusted in supplemented diets. From 1-42 days post-hatch, diet type significantly influenced growth performance. Birds on type C diets had lower growth rates (2,429 vs. 2,631 g/bird; p<0.001), higher feed intakes (4,753 vs. 4,534 g/bird; p<0.005) and less efficient feed conversion (1.96 vs. 1.72; p<0.001) than birds offered type A diets. Enzyme supplementation increased growth rates by 3.2% (2,580 vs. 2,501 g/bird; p<0.005) and improved feed efficiency by 2.7% (1.80 vs. 1.85; p<0.05) over the entire feeding period. There were no interactions between diet type and enzyme supplementation. At 21 days, 5 out of 30 birds per pen were transferred to cages to ascertain treatment effect on apparent metabolisable energy (AME) and nitrogen (N) retention. Xylanase plus phytase enhanced AME (13.48 to 13.91 MJ/kg DM; p<0.001) and N retention (56.3 to 59.7%; p<0.005). Carcass and breast weights of the caged birds were determined following commercial processing. Diet type significantly influenced breast weight, carcass weight and yield. Birds offered Type A diets, in comparison to Type C diets, supported heavier breast (467 vs. 424 g; p<0.001) and carcass weights (1,868 vs. 1,699 g; p<0.001) with superior carcass yields (71.8 vs. 70.6%; p<0.005). Enzyme addition increased carcass weight by 3.9% (1,752 vs. 1,821 g; p<0.005) and breast weight by 5.8% (431 vs. 456 g; p<0.01) without influencing yields. Feed ingredient costs per kg live weight gain and per kg carcass weight indicated that enzyme addition was economically feasible, where supplementation of Type A diets generated the most effective results. Importantly, soluble and total non-starch polysaccharide and phytate contents of the wheat used were typical by local standards. This study confirms the potential of supplementing wheat-based broiler diets with xylanase plus phytase but further investigations are required to define the most appropriate inclusion rates and dietary nutrient specifications in this context.

• Korean Journal of Food Science and Technology
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• v.31 no.4
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• pp.899-905
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• 1999

The lectins from mucilaginous jelly and green epidermis of Aloe vera were isolated by gel and affinity chromatography. The molecular weights of the lectins were determined by SDS-PAGE. The molecular weights of the lectins from mucilaginous jelly isolated by Sephadex G-100 were 58.7 kD and 33.3 kD, and that isolated by acid-treated Sepharose 4B was 176.4 kD. The molecular weights of the lectins from epidermis isolated by Sephadex G-100 were 221.1, 54.0 and 32.5 kD respectively. And that isolated by acid-treated Sepharose 4B was 222.0 and 158.0 kD. The agglutinating activity of lectin from jelly was inhibited by D-galactose, lactose and D-galactosamine, but that from epidermis was not inhibited by lactose. The activity was stable at the pH range of $7.0{\sim}9.0$ and at the temperature $0{\sim}60^{\circ}C$.

• Polymer(Korea)
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• v.28 no.4
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• pp.328-334
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• 2004

A series of methoxy poly(ethylene glycol) (MPEG)-poly(L-lactide-co-glycolide) (PLGA) diblock copolymers were synthesized by ring-opening polymerization of L-lactide and glycolide with carbitol (134 g/mole) or different molecular weights of MPEG (550, 2000, and 5000 g/mole) as an initiator in presence of Sn(Oct)$_2$. The properties of diblock copolymers were characterized by using $^1$H-NMR, GPC, and XRD. After uniform mixing of block copolymers and 1% albumin bovine-fluorescein isothiocyanate(FITC-BSA) with a freeze miller, the wafers loaded FITC-BSA were fabricated by using a mold with a dimensions of 3 mm${\times}$1mm diameter. The release profiles of FITC-BSA and the pH changes of wafer were examined using pH 7.4 PBS for 30 days at 37$^{\circ}C$. The release profiles of albumin showed fast initial burst as the molecular weights of MPEG increased. As a result of this study, the release behavior of BSA was controlled with introducing MPEG in the block copolymers.

• Mycobiology
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• v.29 no.4
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• pp.183-189
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• 2001

Extracellular amylase properties were examined with the mycelium of Tricholoma matsutake isolated from ectomycorrhizal roots of Pinus densiflora. The molecular weights of $\alpha$-amylase and glucoamylase were estimated as 34.2 kD and 11.5 kD, respectively, after eluted through Superdex 75 column. The optimum pH of the purified enzyme was found in a range of pH $5.0{\sim}6.0$, with a peak at pH 5.0. The activities of these enzymes were stable from $4^{\circ}C\;to\;30^{\circ}C$. The $\alpha$-amylase of T. matsutake readily hydrolyzed soluble starch and amylose-B, while it weakly hydrolyzed glycogen, dextrin, amylose and amylose-A. The main products of hydrolysis were confirmed to be glucose, maltose and maltotriose on the basis of the similarities in the thin layer chromatographic mobility.

• Korean Journal of Food Science and Technology
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• v.40 no.1
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• pp.70-75
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• 2008

Two extracellular amylase isozymes were purified and characterized from alkalophilic Pseudomonas sp. KFCC 10818 for the production of maltooligosaccharides. The molecular weights of the homogeneous proteins were 50 kDa and 75 kDa, respectively. The 50 and 75 kDa amylases showed optimum temperatures at 35 and $40^{\circ}C$, respectively. The optimum pH of the enzymes ranged from pH 6-8, and the enzymes were resistant to an alkaline condition of pH 12. Via the enzyme's actions, the final products from maltooligosaccharides or soluble starch were maltose and maltotriose. Calcium was a potent activator of the 50 kDa amylase. Finally, the N-terminal amino acid sequences of the 50 and 75 kDa amylases were QTVPKTTFV and DTVPGNAFQ, respectively.

• Journal of Korea Foresty Energy
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• v.17 no.1
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• pp.56-70
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• 1998

This study was carried out to investigate the structural characteristics of kraft lignin and the wood degrading characteristics, the productivity of ligninolytic enzymes and the enzymatic degradation of kraft lignin by white-rot fungi. To purify kraft lignin, precipitation of kraft pulping black liquors of pitch pine meal was done by titration with lN $H_{2}SO_{4}$ reaching to pH 2, and isolation of the precipitates done by centrifugation. The isolated precipitates from pitch pine were redissloved in lN NaOH, reprecipitated by titration with lN $H_{2}SO_{4}$, washed with deionized water, and kept ofr analysis after freeze drying. Fractionation of the precipitates in solution by successive extraction with $CH_{2}Cl_{2}$ and MeOH, and the fractionates were named SwKL, SwKL I, SwKL II, and SwKL III for pitch pine kraft lignin. The more molecular weights of kraft lignin increased, the less phenolic hydroxyl groups and the more aliphatic hydroxyl groups. Because as the molecular weights increased, the ratio of etherified guaiayl/syringyl(G/S ratio) and the percentage were increased. The spectra obtained by 13C NMR and FTIR assigned by comparing the chemical shifts of various signals with shifts of signals from autherized ones reported. The optimal growth temperature and pH of white-rot fungi in medium were $28^{\circ}C$ and 4.5-5.0, respectively. Especially, in temperature and pH range, and mycelial growth, the best white-rot fungus selected was Phanerochaete chrysosporium for biodegradation. For the degradation pathways, the ligninolytic fungus jcultivated with stationary culture using medium of 1% kraft lignin as a substrate for 3 weeks at $28^{\circ}C$. The weight loss of pitch pine kraft lignin was 15.8%. The degraded products extracted successively methoanol, 90% dioxane and diethyl ether. The ether solubles were analyzed by HPLC. Kraft lignin degradation was initiated in $\beta$-O-4 bonds of lignin by the laccase from Phanerochaete chrysosporium and the degraded compounds were produced from the cleavage of $C\alpha$-$C\beta$ linkages at the side chains by oxidation process. After $C\alpha$-$C\beta$ cleavage, $C\alpha$-Carbon was oxidized and changed into aldehyde and acidic compounds such as syringic acid, syringic aldehyde and vanilline. And the other compound as quinonemethide, coumarin, was analyzed. The structural characteristics of kraft lignin were composed of guaiacyl group substituted functional OHs, methoxyl, and carbonyl at C-3, -4, and -5 and these groups were combinated with $\alpha$ aryl ether, $\beta$ aryl ether and biphenyl. Kraft lignin degradation pathways by Phanerochaete chrysosporium were initially accomplished cleavage of $C\alpha$-$C\beta$ linkages and $C\alpha$ oxidation at the propyl side chains and finally cleavage of aromatic ring and oxidation of OHs.

• Communications of the Korean Mathematical Society
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• v.10 no.4
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• pp.881-887
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• 1995

Let f be a measurable function on the unit ball B in $C^n$, then we define a maximal function $M_p(f), 1 \leq p < \infty$, by $$ M_p(f)(\zeta ) = \sup_{\delta > 0}(\frac{1}{\sigma(\beta(\zeta, \delta))} \int_{T(\beta(\zeta, \delta))} $\mid$f(z)$\mid$^p \frac{d\nu(z)}{(1-$\mid$z$\mid$^n})^{1/p} $$ where $\sigma$ denotes the surface area measure on S, the boundary of B, and $T(\beta(\zeta, \delta))$ denotes the tent over the ball $\beta(\zeta, \delta)$. We prove that the maximal operator $M_p$ belongs to the Muckenhoupt class $A_1$.

• Communications of the Korean Mathematical Society
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• v.35 no.4
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• pp.1159-1170
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• 2020

We consider the weighted spaces ℓ^p(𝕊, 𝜑) and ℓ^p(𝕊, 𝜓) for 1 < p < +∞, where 𝜑 and 𝜓 are weights on 𝕊 (= ℕ or ℤ). We obtain a sufficient condition for ℓ^p(𝕊, 𝜓) to be multiplier weighted-space of ℓ^p(𝕊, 𝜑) and ℓ^p(𝕊, 𝜓). Our condition characterizes the last multiplier weighted-space in the case where 𝕊 = ℤ. As a consequence, in the particular case where 𝜓 = 𝜑, the weighted space ℓ^p(ℤ,𝜓) is a convolutive algebra.