scholarly journals Homogeneous Distribution of Polymerizable Coumarin Dyes for Active Few Mode POF

Materials ◽  
2020 ◽  
Vol 13 (8) ◽  
pp. 1975
Author(s):  
Florian Jakobs ◽  
Kristoffer Harms ◽  
Jana Kielhorn ◽  
Daniel Zaremba ◽  
Pen Yiao Ang ◽  
...  
Keyword(s):  
Methyl Methacrylate ◽  
Optical Fibers ◽  
High Performance ◽  
Polymer Chains ◽  
Size Exclusion ◽  
Polymerization Process ◽  
Homogeneous Distribution ◽  
Exclusion Chromatography ◽  
Polymer Optical Fibers ◽  
Coumarin Dyes

For most kinds of active polymer optical fibers, a homogeneous distribution of dye molecules over the entire fiber length and cross section is required. In this study, chemical bonding of dyes to poly(methyl methacrylate) (PMMA) by copolymerization is achieved within the polymerization process instead of dissolving the dyes in the monomers. In combination with an improved fabrication mechanism, this leads to homogeneous dye distribution within the preforms. A method for proving the integration of the dyes into the polymer chains has been developed using high-performance liquid chromatography (HPLC) and size exclusion chromatography (SEC). Prestructured core-cladding preforms with dye-doped poly(cylohexyl methacrylate-co-methyl methacrylate)-core have been prepared with the Teflon string technique and were heat-drawn to few mode fibers.

scholarly journals Periplasmic synthesis and purification of the human prolactin antagonist Δ1-11-G129R-hPRL

AMB Express ◽  
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Miriam F. Suzuki ◽  
Larissa A. Almeida ◽  
Stephanie A. Pomin ◽  
Felipe D. Silva ◽  
Renan P. Freire ◽  
...  
Keyword(s):  
Size Exclusion Chromatography ◽  
High Performance ◽  
Signal Sequence ◽  
Osmotic Shock ◽  
Size Exclusion ◽  
Specific Expression ◽  
E Coli ◽  
Human Prolactin ◽  
Exclusion Chromatography

AbstractThe human prolactin antagonist Δ1-11-G129R-hPRL is a 21.9 kDa recombinant protein with 188 amino acids that downregulates the proliferation of a variety of cells expressing prolactin receptors. Periplasmic expression of recombinant proteins in E. coli has been considered an option for obtaining a soluble and correctly folded protein, as an alternative to cytoplasmic production. The aim of this work was, therefore, to synthesize for the first time, the Δ1-11-G129R-hPRL antagonist, testing different activation temperatures and purifying it by classical chromatographic techniques. E. coli BL21(DE3) strain was transformed with a plasmid based on the pET25b( +) vector, DsbA signal sequence and the antagonist cDNA sequence. Different doses of IPTG were added, activating under different temperatures, and extracting the periplasmic fluid via osmotic shock. The best conditions were achieved by activating at 35 °C for 5 h using 0.4 mM IPTG, which gave a specific expression of 0.157 ± 0.015 μg/mL/A600 at a final optical density of 3.43 ± 0.13 A600. Purification was carried out by nickel-affinity chromatography followed by size-exclusion chromatography, quantification being performed via high-performance size-exclusion chromatography (HPSEC). The prolactin antagonist was characterized by SDS-PAGE, Western blotting, reversed-phase high-performance liquid chromatography (RP-HPLC) and MALDI-TOF–MS. The final product presented > 95% purity and its antagonistic effects were evaluated in vitro in view of potential clinical applications, including inhibition of the proliferation of cancer cells overexpressing the prolactin receptor and specific antidiabetic properties, taking also advantage of the fact that this antagonist was obtained in a soluble and correctly folded form and without an initial methionine.

Using HPSEC to identify NOM fraction removal and the correlation with disinfection by-product precursors

2015 ◽  
Vol 16 (2) ◽  
pp. 305-313 ◽  
Author(s):  
Euis Nurul Hidayah ◽  
Yung-Chen Chou ◽  
Hsuan-Hsien Yeh
Keyword(s):  
Humic Substances ◽  
Natural Organic Matter ◽  
High Performance ◽  
Haloacetic Acids ◽  
Size Exclusion ◽  
Formation Potential ◽  
Trihalomethane Formation Potential ◽  
Exclusion Chromatography ◽  
Alum Coagulation ◽  
Aliphatic Biopolymer

In this study high performance size exclusion chromatography (HPSEC) was used to compare an ultrafiltration (UF) membrane and alum coagulation for their capacity to remove different fractions of natural organic matter (NOM) from water. At the same time, the removal of disinfection by-product (DBP) precursors, as measured by trihalomethane formation potential (THMFP) and haloacetic acid formation potential (HAAFP), was also detected. The results show that the UF membrane mainly removed the aliphatic biopolymer fraction, while alum coagulation mainly removed the humic substances fraction. The results of DBP precursor analysis show that more THMFP was removed by the UF membrane than HAAFP, while the reverse was true for alum coagulation. It is conjectured that the aliphatic biopolymer fraction is the major precursor for trihalomethanes (THMs), while the humic substances fraction is the major precursor for haloacetic acids (HAAs).

scholarly journals Ultra-high performance size-exclusion chromatography of synthetic polymers

2013 ◽  
Vol 36 (17) ◽  
pp. 2718-2727 ◽  
Author(s):  
Miroslav Janco ◽  
James N. Alexander ◽  
Edouard S. P. Bouvier ◽  
Damian Morrison
Keyword(s):  
Size Exclusion Chromatography ◽  
High Performance ◽  
Synthetic Polymers ◽  
Size Exclusion ◽  
Exclusion Chromatography

Molecular and biochemical characteristics of inulosucrase InuBK from Alkalihalobacillus krulwichiae JCM 11 691

2021 ◽  
Author(s):  
Ken-ji Yokoi ◽  
Sosyu Tsutsui ◽  
Gen-ya Arakawa ◽  
Masakazu Takaba ◽  
Koichi Fujii ◽  
...  
Keyword(s):  
High Performance ◽  
Culture Medium ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Resonance Spectroscopy ◽  
Gene Encoding ◽  
Reading Frame ◽  
Exclusion Chromatography ◽  
Chain Lengths

Abstract Information about the inulosucrase of non-lactic acid bacteria is scarce. We found a gene encoding inulosucrase (inuBK) in the genome of the gram-positive bacterium Alkalihalobacillus krulwichiae JCM 11691. The inuBK open reading frame encoded a protein comprising 456 amino acids. We expressed His-tagged InuBK in culture medium using a Brevibacillus system. The optimal pH and temperature of purified InuBK were 7.0–9.0 and 50 °C–55 °C, respectively. The findings of high-performance anion-exchange chromatography, nuclear magnetic resonance spectroscopy, and high-performance size-exclusion chromatography with multi-angle laser light scattering showed that the polysaccharide produced by InuBK was an inulin with a molecular weight of 3,806, a polydispersity index (PI) of 1.047, and fructosyl chain lengths with 3–27 degrees of polymerization. The size of InuBK was smaller than commercial inulins, and the PI of the inulin that it produced was lower.

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