Pembuatan Aplikasi Sistem Informasi Persebaran Toko Batik Di Kota Pekalongan Berbasis Android

Pekalongan is located in the lowlands along the north coast of Java Island, at a height of approximately one meter above sea level. The geographical position of Pekalongan is between 6° 50\u27 42" to 6° 55\u27 44\u27\u27 North Latitude and 109° 37\u27 55\u27\u27to 109° 42\u27 19\u27\u27 East Longitude.Pekalongan area of about 42.25 km2 or approximately 0.14% from the area of Central Java Province.Pekalongan is known by the nickname city of Batik, because batik Pekalongan has distinctive and varied livery. Therefore, Pekalongan is espected to provide a practical and informative information for tourists, so it can be an attraction and increase the number of tourists coming to Pekalongan. This research uses of spatial and non spasial data in the form of batik store name, the owner\u27s name, phone number, address, and products sold with using the popularity of android smartphone as a platform system information.This application was developed using an SDK Andoidframework, java and PHP programming languages, and MySQL as base data, and Google Maps. The final result of this research is the Android application of the distribution of batik store in Pekalongan is accompanied by information (as has been mentioned above) from each store for easier searching the location of the batik stores in Pekalonga

Selective Inactivation of Serine Proteases by Nonheme Iron Complexes

Oxidative inactivation of the serine proteases trypsin and chymotrypsin by nonheme iron complexes is described. The nonheme ligands N4Py (1) and derivative 3CG-N4Py (2), which contains a pendant guanidinium group, were used as ligands for iron. Ferryl (FeIVO) species derived from these ligands, [FeIV(O)(N4Py)]2+ (7) and [FeIV(O)(3CG-N4Py)]3+ (8), inactivate trypsin and chymotrypsin by the oxidation of amino acid side chains. Ferryl 8 is most effective with chymotrypsin (IC50 value of 26 μM for 8 vs 119 μM for 7). IC50 values of 71 and 54 μM were obtained for trypsin with 7 and 8, respectively. Amino acid analysis confirmed that residues cysteine, tyrosine, and tryptophan are oxidized under these conditions. Trypsin is inactivated preferentially over chymotrypsin under catalytic conditions, where the enzyme was pulsed with H2O2 in the presence of ferrous complexes [FeII(OH2)(N4Py)]2+(5) and [FeII(Cl)(3CG-N4Py)]2+ (6). Control experiments support the action of a unique oxidant, other than ferryls or hydroxyl radicals, under these conditions, where tyrosine residues are targeted selectively

Synthesis, Characterization, and Glutathionylation of Cobalamin Model Complexes [Co(N4PyCO₂Me)Cl]Cl₂ and [Co(Bn-CDPy3)Cl]Cl₂

Synthetic Co­(III) complexes containing N5 donor sets undergo glutathionylation to generate biomimetic species of glutathionylcobalamin (GSCbl), an important form of cobalamin (Cbl) found in nature. For this study, a new Co­(III) complex was synthesized derived from the polypyridyl pentadentate N5 ligand N4PyCO₂Me (<b>1</b>). The compound [Co­(N4PyCO₂Me)­Cl]­Cl₂ (<b>3</b>) was characterized by X-ray crystallography, UV–vis, IR, ¹H NMR, and ¹³C NMR spectroscopies and mass spectrometry (HRMS). Reaction of <b>3</b> with glutathione (GSH) in H₂O generates the biomimetic species [Co­(N4PyCO₂Me)­(SG)]²⁺ (<b>5</b>), which was generated <i>in situ</i> and characterized by UV–vis and ¹H NMR spectroscopies and HRMS. ¹H NMR and UV–vis spectroscopic data are consistent with ligation of the cysteine thiolate of GSH to the Co­(III) center of <b>5</b>, as occurs in GSCbl. Kinetic analysis indicated that the substitution of chloride by GS^– occurs by a second-order process [<i>k</i>₁ = (10.1 ± 0.7) × 10^–2 M^–1 s^–1]. The observed equilibrium constant for formation of <b>5</b> (<i>K</i>_obs = 870 ± 50 M^–1) is about 3 orders of magnitude smaller than for GSCbl. Reaction of the Co­(III) complex [Co­(Bn-CDPy3)­Cl]­Cl₂ (<b>4</b>) with GSH generates glutathionylated species [Co­(Bn-CDPy3)­(GS)]²⁺ (<b>6</b>), analogous to <b>5</b>. Glutathionylation of <b>4</b> occurs at a similar rate [<i>k</i>₂ = (8.4 ± 0.5) × 10^–2 M^–1 s^–1], and the observed equilibrium constant (<i>K</i>_obs = 740 ± 47 M^–1) is slightly smaller than for <b>5</b>. Glutathionylation showed a significant pH dependence, where rates increased with pH. Taken together, these results suggest that glutathionylation is a general reaction for Co­(III) complexes related to Cbl

Water Challenges in South Asian Countries: A Focused Review on Emerging Nanomaterials and Technological Processes in Wastewater Treatment

South Asia, the world’s most populated region, is facing many environmental and healthcare challenges due to poor freshwater management/wastewater treatment. Most South Asian (SA) countries, such as India, Pakistan, Sri Lanka, and Bangladesh, are suffering from water pollution issues generated due to domestic and industrial effluents containing heavy/toxic ions, textile dyes, pharmaceuticals, bacteria/viruses inorganic/organic pollutants, etc. To overcome these challenges, extensive research is being carried out with an emphasis on technological development to maintain water sustainability. The present review discusses water pollution as well as various challenges in SA countries along with solutions through scientific research carried out by developing nanomaterials and technological wastewater treatment processes, i.e., photocatalytic/adsorptive removal, disinfection, tracing/sensing, etc. Particularly, syntheses of TiO2 nanoparticles and graphene oxide (GO)-based nanomaterials which were found to be most extensively investigated in the SA region have been discussed with emphasis on their multifunctional applications using various water treatment processes, mechanisms, and synergetic effects. Eventually, various challenging issues and solution opportunities are discussed for future development to maintain water sustainability in SA countries

Data for: Synthesis, crystal structure, and electronic structure of Ba2GeTe3(Te2) Jai Prakasha, Adel Mesbahb, Sébastien Lebègued, and James A. Ibers

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Schematic representation of the prokaryotic vectors used for the expression of the recombinant proteins.

<p>IFNγ (<b>A</b>) and mimetic IFNγ (<b>B</b>) were cloned in-frame upstream of His-tag in pET42a (+) vector to achieve cytoplasmic protein expression. The fusion proteins BiPPB-IFNγ (<b>C</b>) and BiPPB-mimIFNγ (<b>D</b>) were expressed in pET39b (+) vector for periplasmic expression of fusion proteins to ensure proper folding and disulfide bonds formation. For the synthesis of fusion proteins, BiPPB was fused to the N-terminal of IFNγ or mimetic IFNγ sequence through a flexible 3 amino acid linker (AAA) maintaining the open reading frame.</p

Dot-blot and <i>in vitro</i> binding of recombinant proteins in human HSC.

<p>(<b>A</b>) Dot-blot analysis of purified recombinant proteins IFNγ, mimetic IFNγ, BiPPB-IFNγ and BiPPB-mimIFNγ using anti-IFNγ and anti-PPB antibody. (<b>B</b>) Representative pictures showing binding of BiPPB-IFNγ and BiPPB-mimIFNγ to human HSC (LX2). Mouse IFNγ and mimIFNγ did not show any binding (similar to control) to human LX2 cells due to species differences and lack of IFNγR or PDGFβR binding sites respectively.</p

Effects of recombinant proteins on fibrotic parameters in vivo.

<p>(<b>A</b>) Representative pictures of collagen I and α-SMA stained liver sections from olive oil treated mice (normal) or CCl₄-treated mice (acute model) that were treated with IFNγ (n = 6), MimIFNγ (n = 5), BiPPB-IFNγ (n = 6), BiPPB-mimIFNγ (n = 6) or PBS alone (n = 6). Scale bars, 200 µm. (<b>B</b>) Whole-liver lysates from treated animals were subjected to western blot analysis using anti-collagen I antibody. Graph represents collagen I expression (normalized with β-actin) depicted as mean ± SEM from n = 5–6 mice per group. #P<0.05 denotes significance versus PBS treated olive oil mice and *P<0.05, **P<0.01 denotes significance versus PBS treated-CCl₄ mice. For quantitative analysis, the groups were normalized to vehicle group (PBS treated-CCl₄ mice). (<b>C</b>) Effect of recombinant proteins on intrahepatic fibrinolysis as determined by the ratio of MMP13 and TIMP-1 transcripts. The groups were normalized to vehicle group (PBS treated-CCl₄ mice). Bars represent mean ± SEM of 5–6 mice per group. *P<0.05, **P<0.01 denotes significance versus PBS treated-CCl₄ mice.</p

Effect of 15d-PGJ₂ and its analog CAY-10410 on SIRT1 and HDAC1 activity.

<p>(<b>A</b>) Chemical structures of 15d-PGJ₂ (15-deoxy-Δ^12,14-Prostaglandin J₂) and its analog CAY-10410 (9,10-dihydro-15-deoxy-Δ^12,14-Prostaglandin J₂). Asterisk indicates the electrophilic carbon atoms which might be involved in Michael addition reaction. Panel (<b>A</b>) and (<b>B</b>) show the concentration-dependent effects of 15d-PGJ₂, CAY-10410 and ciglitazone on the deacetylase activity of SIRT1 and HDAC1, respectively using <i>in vitro</i> enzyme assays. ^#P<0.01 versus ciglitazone, ^†p<0.05 and ^††p<0.01 versus CAY-10410. (<b>D</b>) Effect of CAY-10410 on the cell viability of A2780 and A2780/AD cells as measured with an alamar blue assay. (<b>E</b>) Treatment with CAY-10410 (2.5 µM) did not induce cell transformation after 48 h incubation. Magnification, 200×.</p

Effects of recombinant proteins on IFNγ-related adverse effect in the acute CCl₄ model.

<p>Graph represents platelet counts measured in CCl₄-treated mice receiving PBS (n = 6) or the different recombinant proteins IFNγ (n = 6), MimIFNγ (n = 5), BiPPB-IFNγ (n = 6), BiPPB-mimIFNγ (n = 6). Bars represent mean ± SEM of 5–6 mice per group. The results showed a significant reduction in platelet counts following two intravenous administration of IFNγ, which was significantly improved following treatment with BiPPB-mimIFNγ and to a lesser extent with BiPPB-IFNγ. MimIFNγ did not show significant change in platelets counts due to lack of binding to IFNγR or PDGFβR. *P<0.05, **P<0.01 denotes significance versus PBS treated CCl₄ mice. #P<0.05 denotes the significance versus IFNγ-treated CCl₄ mice.</p