There is a dire need to find an efficient, cost-effective, sustainable, and environment-friendly adsorbent for the removal of anionic pollutants such as dyes from waste effluent. In this work, a cellulose-based cationic adsorbent was designed and utilized for methyl orange and reactive black 5 anionic dyes adsorption from an aqueous medium. Solid-state nuclear magnetic resonance spectroscopy (NMR) revealed the successful modification of cellulose fibers, and dynamic light scattering (DLS) evaluations showed the levels of charge densities.
View Article and Find Full Text PDFThe objective of this study was to evaluate the seminal traits and sexual behaviors of mature Brahman bulls in a multi-sire system during mating or resting seasons and different climatic periods of the year at the Colombian flooded savannas. Thirty-two Brahman bulls, suitable for reproduction, were used, which were subjected to breeding soundness evaluation, as well as the libido and service capacity tests. Such evaluations were compared among different seasons of the year in relation to the rainfall.
View Article and Find Full Text PDFFolate receptor is over-expressed in a variety of carcinomas. To design a cytotoxic drug that would selectively target these carcinomas, we synthesized folate-maytansinoids. These drugs showed high affinity toward folate receptor, appeared to enter cells exclusively via the folate receptor-mediated caveolar pathway and displayed high cytotoxic potency (in the range of 10[-11] to 10[-10] M) and remarkable selectivity for folate receptor-expressing carcinoma cell lines.
View Article and Find Full Text PDFExpression plasmids carrying a humanized N901 immunoglobulin heavy chain gene (hN901HC) fused to a gene encoding the native B chain of ricin toxin (RTB), hN901HC-RTB, or a sugar binding mutant of RTB, hN901HC-RTB delta gly, were constructed. In each case, the fused gene constructions were co-expressed in murine myeloma cells (Sp2/0) with the gene for humanized N901 immunoglobulin light chain to produce the secreted recombinant products hN901-RTB and hN901-RTB delta gly, respectively. When purified by affinity chromatography, both the hN901-RTB and hN901-RTB delta gly products were found to have an apparent molecular mass of M(r) = 210,000 and to be composed of two hN901 antibody heavy chains each fused to a full-length copy of RTB and two hN901 antibody light chains.
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