scholarly journals Development of the Synthesis of 2,4-Di(α-methoxyethyl)- deuteroporphyrin IX Ytterbium Complex Dipotassium Salt

2019 ◽  
Vol 12 (4) ◽  
pp. 382-388 ◽  
Author(s):  
Anastasiya E. Shchelkunova ◽  
Ekaterina V. Boltukhina ◽  
Valentina D. Rumyantseva ◽  
Igor’ P. Shilov ◽  
Salis D. Karakotov
Keyword(s):  
1962 ◽  
Vol 8 (1) ◽  
pp. 49-56 ◽  
Author(s):  
J. M. Ingram ◽  
A. C. Blackwood

The biosynthesis of pyocyanine, the blue phenazine pigment produced by Pseudomonas aeruginosa, was studied by the addition of radioactive substrates to a culture growing on a complete medium. The distribution of labelled carbon from radioactive substrates in the pyocyanine was examined by degrading the pigment to 1-hydroxyphenazine, quinoxaline dicarboxylic acid, quinoxaline, and pyrazine tetracarboxylic acid dipotassium salt, and thus 7 of the 13 carbons were assayed separately or in pairs.Glycerol-1,3-C14 is the principal donor of radioactivity to the pyocyanine carbon, but not all the carbon atoms tested were labeled. Alanine-U-C14 contributed carbon to pyocyanine also, but not to all carbons, and at a much lower level of efficiency than glycerol. However, with leucine-U-C14, all carbon atoms tested were labeled to a slight extent. These amino acids, when labeled specifically, and glutamate-U-C14, oxalic acid-C14, and sodium formate-C14 did not contribute significantly to pyocyanine carbon.The distribution of radioactivity from glycerol in the pyocyanine molecule suggests the pigment is formed from glycerol or a product closely related to it by the condensation of two carbon units or the condensation of four and two carbon units.


2005 ◽  
Vol 340 (15) ◽  
pp. 2422-2427 ◽  
Author(s):  
Lucjan B. Jerzykiewicz ◽  
Tadeusz Lis ◽  
Ewa Zuziak
Keyword(s):  
X Ray ◽  

2017 ◽  
Vol 8 (1) ◽  
pp. 337-343 ◽  
Author(s):  
Vladimir A. Burilov ◽  
Diana A. Mironova ◽  
Regina R. Ibragimova ◽  
Vladimir G. Evtugyn ◽  
Yurii N. Osin ◽  
...  

2019 ◽  
Vol 97 (6) ◽  
pp. 504-511
Author(s):  
Srabani Karmakar ◽  
Shrutidhara Biswas ◽  
Kali P. Das ◽  
Umakanta Tripathy

α-Crystallin, an abundant mammalian lens protein made up of two subunits (αA- and αB-crystallin), is involved in the maintenance of the optimal refractive index in the lens. The protein is implicated in the pathophysiology of a large number of retinal diseases including cataract, age-related macular degeneration, diabetic retinopathy, and uveitis. α-Crystallin belongs to the small heat shock protein (sHSP) family, forms large oligomeric structures, and functions as a molecular chaperone appearing very early during embryonic development. To gain mechanistic insight into the structural and functional role of α-crystallin and its alterations in various retinal diseases, it is important to study the interaction chemistry with its known partners. The hydrophobic sites in α-crystallin have been studied extensively using environmentally sensitive fluorescent probes such as 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) that interacts with both subunits of α-cystallin in 1:1 stoichiometry at 37 °C and diminishes the chaperone-like activity of the protein. Furthermore, it has been shown that ATP plays a crucial role in the association of α-crystallin with substrate proteins. We use surface plasmon resonance (SPR) to monitor the interactions of immobilized oligomeric recombinant αA subunit of human α-crystallin protein with bis-ANS and ATP. We assess the thermodynamic parameters and kinetics of such interactions at various temperatures. Our results indicate that bis-ANS binds to αA-crystallin with higher affinity when compared with ATP, although both αA-crystallin and αB-crystallin display fast interaction kinetics.


Author(s):  
Md. Shahidul Islam ◽  
Trevor D. Hunt ◽  
Zhiqian Liu ◽  
Kym L. Butler ◽  
Tony M. Dugdale

Endothall dipotassium salt and monoamine salt are herbicide formulations used for controlling submerged aquatic macrophytes and algae in aquatic ecosystems. Microbial activity is the primary degradation pathway for endothall. To better understand what influences endothall degradation, we conducted a mesocosm experiment to (1) evaluate the effects of different water and sediment sources on degradation, and (2) determine if degradation was faster in the presence of a microbial community previously exposed to endothall. Endothall residues were determined with LC-MS at intervals to 21 days after endothall application. Two endothall isomers were detected. Isomer-1 was abundant in both endothall formulations, while isomer-2 was only abundant in the monoamine endothall formulation and was more persistent. Degradation did not occur in the absence of sediment. In the presence of sediment, degradation of isomer-1 began after a lag phase of 5–11 days and was almost complete by 14 days. Onset of degradation occurred 2–4 days sooner when the microbial population was previously exposed to endothall. We provide direct evidence that the presence and characteristics of sediment are of key importance in the degradation of endothall in an aquatic environment, and that monoamine endothall has two separate isomers that have different degradation characteristics.


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