UJI RESISTENSI PRIMER MYCOBACTERIUM TUBERCULOSIS TERHADAP INH (ISONICOTINYL HYDRAZIDE) PADA PENDERITA TUBERCULOSIS

Latar belakang dari penelitian ini bahwa jumlah penderita TB berdasarkan data yang diperoleh dari Balai Besar Kesehatan Paru Masyarakat di Makassar pada tahun 2010, jumlah kasus TB adalah 4944 dan pada tahun 2011 dari bulan januari sampai bulan November adalah 5368. Dari data BBKPM Makassar pada tahun 2017 suspek penderita TB MDR berjumlah 2224 pasien dan penderita TB MDR berjumlah 24 pasien . Penelitian ini telah dilaksanakan pada BBKM Makassar dengan teknik pengambilan sampel menggunakan Purposive sampling cara dengan ciri – ciri yang ditetapkan sampai jumlah kuota yang telah ditentukan tercukupi . Jenis penelitian ini adalah penelitian observasi laboratorik yang bersifat deskriptif, yang bertujuan untuk mengetahui hasil deteksi resistensi primer Mycobacterium tuberculosis terhadap INH (Isonicotinyl hydrazide) pada penderita tuberkulosis yang baru memulai pengobatan dengan metode PCR. Hasil penelitian menunjukkan bahwa, dari 13 sampel yang diamplifikasi, didapatkan 4 (31%) sampel sputum penderita tuberkulosis yang baru memulai pengobatan resisten terhadap INH dan 9 (69%) sampel sputum penderita tuberkulosis yang baru memulai pengobatan sensitive terhadap INH dan terjadinya resistensi Mycobacterium tuberculosis terhadap INH dipengaruhi oleh mutasi pada beberapa gen , mutasi ini terutama terjadi pada gen katG, gen inhA, dan gen ahpC. Untuk penelitian selanjutnya disarankan dengan menggunakan sampel yang lebih banyak dan mencakup daerah yang lebih luas.Kata Kunci : Mycobacterium tuberculosis , Resistensi Primer , INH , Penderita Tuberkulosis, PCR

X-ray crystal structure of N'-[(1E)-1-(2,4-dihydroxyphenyl)-ethylidene]pyridine-4-carbohydrazide

Schiff’s base of isonicotinyl hydrazide with 2’,4’-dihydroxy acetophenone (INH-RA) has been designed and synthesized as a part of library enumeration targeting the NS2B-NS3 protease of Dengue virus. Slow evaporation from methanol results in the formation of monoclinic crystals C2/c space group with eight molecules in the unit cell (a=20.0165(3) Å, b=7.7594(10) Å, c=19.4809(3) Å, α=90 °, β=111.368(1) °, γ=90 ° and Z=8).Three dimensional X-ray crystallographic structure of the compound has been determined and refined using SHELXS-97 and SHELXL-2014, respectively to a final R-value of 4.64%

Preparation of an In Situ Crosslinked Polymer Coating and a Double-Layered Thermal CTP Plate

The research relates to a method for preparing an in-situ crosslinked polymer coating. It has excellent solubility in aqueous alkaline solution, but didnt dissolve in general organic solvents and water. The crosslinked polymer coating was made through the reaction of a copolymer derived from diacetone acrylamide (DAAM) and ethacryloyloxyethyl-carbazochrome-p-toluenesulfonamide (MCTS) with a crosslinking agent, isonicotinyl hydrazide. The two components were dissolved in 3-methoxypropanol to prepare the coating solution, which was then coated to a grained and anodized aluminum substrate and dried at 120 °C for 5 min to obtain the crosslinked coating. There exists intermolecular hydrogen bond between the pyridine ring of isonicotinyl hydrazide and the sulfonamide group of the MCTS unit of the copolymer. The reaction between the hydrazide group and the carbonyl group during the drying process generated the hydrazone bond, resulting in the crosslinked polymer coating. The intermolecular hydrogen bond and the covalent bond render the coating insoluble in most organic solvents. However, the hydrogen bond was readily broken down when the coating was exposed to aqueous alkaline solution due to the ionization of the sulfonamide group, causing rapid dissolution of the coating. The coating was also used as the under-layer for the preparation of a double-layed CTP plate. The performance of the double-layed CTP plate was preliminarily studied.

Effect of photorespiratory inhibitors on in vivo nitrate reduction in the leaves of barley and maize

The effects of photorespiratory inhibitors, α-hydroxypyridinemethanesulphonate, isonicotinyl hydrazide, and amino-oxyacetate, on in vivo nitrate reduction in the leaves of barley (C3) and maize (C4) were studied. The inhibitors had a pronounced effect on enzyme activity in the leaves of barley but not of maize. Photorespiratory substrates, glycolate and glycine, enhanced nitrate reduction in the leaves of barley. The enhancement was reversed by the inhibitors. It is proposed that glycine oxidation supports nitrate reduction in C3 plants but not in C4 plants.

Stimulation of Photorespiration by the Carbonic Anhydrase Inhibitor Ethoxyzolamide in Chlorella vulgaris

Ammonia was excreted at high rates in the presence of L-methionine sulfoximine (L-MSO) from Chlorella cells which have been grown and analyzed at normal CO2 partial pressure (330 ppm ). If these cells are analyzed at high CO2-concentration (3% CO2 in air) only little ammonia is excreted in the presence of L-MSO. In the absence of L-MSO no ammonia is excreted under either condition. In agreem ent with this observation Chlorella cells grown under high CO2 partial pressure (3% CO2 in air) but tested under normal CO2 partial pressure excreted only very little ammonia. Under these conditions neither “High CO2-cells” nor “Low CO2-cells” exhibited any glycolate excretion. However, glycolate excretion was observed in the presence of a-HPMS (a-hydroxy-2-pyridyl methanesulfonate) an inhibitor of glycolate dehydrogenase or INH (isonicotinyl hydrazide) an inhibitor of the glycine-serine am inotransferase, irrespective of the presence or absence of L-M SO. INH inhibited ammonia excretion. The above described high ammonia excretion in “Low CO2-cells” in the presence of L-MSO was suppressed or substantially reduced by 0.1 mм ethoxyzolamide an inhibitor of carbonic anhydrase which, however, at the same time caused a substantial excretion of glycolate into the medium. The same qualitative effect of ethoxyzolam ide was observed in “High CO2-cells” (tested under normal CO2 partial pressure) although the amount of glycolate excreted in this type of culture was very small. It was generally noted that glycolate excretion caused by ethoxyzolamide was stoichiometrically always more important than the rate of ammonia excretion which was inhibited. This shows that excretion and therefore most probably also the formation of glycolate are enhanced by ethoxyzolamide. The experiments seem to show that due to the inhibition of carbonic anhydrase the affinity of the ribulose-1,5-bisphosphate carboxylase/oxygenase system is increased towards oxygen, which leads to a stimulation of the photorespiratory carbon cycle.

Aminotransferase-Aktivität in der Blaualge Anacystis nidulans / Activity of Aminotransferases in the Blue Green Alga Anacystis nidulans

The blue-green alga Anacystis nidulans (strain L 1402-1) was grown at + 37 °C in air (0.03 vol.% CO2 and in air enriched with 3.0 vol.% CO2. The effects of several inhibitors on the activity of aminotransferases, 14CO2 fixation and radioactive photosynthetic products of Anacystis were studied. No serine-pyruvate aminotransferase activity could be found in 10-2 м isonicotinyl hydrazide (INH) ; under the influence of this inhibitor aspartate and alanine aminotransferase were decreased about 49% respectively 17.6%. Serine-pyruvate and alanine aminotransferase activity decreased to more than 50% in 10-3 м glyoxalbisulfite. The obtained inhibitory effect of 10-4 м HPMS on serine-piruvate aminotransferase (35%) was stronger than on the other aminotransferases. DCMU (5 × 10-6 м) inhibition on alanine aminotransferase activity was 83.7%. Under the influence of 10-3 м glyoxalbisulfite no 14C-labelled amino acids could be detected after 5 min photosynthesis; 14C-labelling of phosphoenolpyruvate, malate, phosphoglycolate and glycolic acid increased. Isonicotinyl hydrazide (10-2 м) caused in comparison to the control experiment a lower radioactivity in aspartate, glutamate and phosphoenolpyruvate. The results are discussed with reference to the operation of the glycolate pathway and a carboxylation reaction of phosphoenolpyruvate in the blue-green alga Anacystis nidulans.