scispace - formally typeset
Search or ask a question
Topic

Chemical binding

About: Chemical binding is a research topic. Over the lifetime, 1822 publications have been published within this topic receiving 52516 citations.


Papers
More filters
Journal ArticleDOI
Zhenya Luo1, Meiling Peng1, Weixin Lei1, Yong Pan1, Youlan Zou1, Zengsheng Ma1 
TL;DR: In this paper, a kind of binder-free CNTs/(Ni-P)/Sn composites are designed and electroplated on Cu current collector as anodes for lithium-ion battery.

9 citations

Journal Article
TL;DR: CDDP-induced inhibition of the Na+/glucose cotransport system is mainly mediated by direct chemical binding of cDDP and/or its hydrated derivatives to essential sulfhydryl groups of the transport protein and may also involve other nucleophilic groups (e.g., the -SCH3 group of methionines).
Abstract: The potent anticancer drug cis -diamminedichloroplatinum (II) (cDDP) impairs glucose reabsorption by renal proximal tubular cells, which leads to glucosuria. We investigated the direct effect of cDDP (0.04–2 mM) on the Na + /glucose cotransport system in brush-border membrane (BBM) vesicles from the rabbit renal cortex. cDDP induced 1) concentration-dependent inhibition of the Na + /glucose cotransport system, by decreasing its V max value and, to a lesser extent, its affinity, and 2) platinum binding to BBM vesicles, associated with decreases in protein-bound thiols. cDDP produced weaker inhibition of the Na + /glucose cotransport system and platinum binding to BBM vesicles than did highly reactive cDDP hydrated derivatives, with similar decreases in protein-bound thiols. Treatment with diethyldithiocarbamic acid (a drug protecting against cDDP nephrotoxicity), immediately after cDDP exposure, 1) partially lifted the cDDP-induced inhibition of the Na + /glucose cotransporter, 2) reduced platinum binding to BBM vesicles, but 3) did not modify the cDDP-induced decrease in protein-bound thiols. Our findings strongly suggest that cDDP-induced inhibition of the Na + /glucose cotransport system is mainly mediated by direct chemical binding of cDDP and/or its hydrated derivatives to essential sulfhydryl groups of the transport protein and may also involve other nucleophilic groups ( e.g., the -SCH 3 group of methionines).

9 citations

Journal ArticleDOI
TL;DR: In this article, the ion microprobe mass analyzer (IMMA) was used for microchemical analysis in situ of all important elements in soil specimens and the results showed that all chemical elements could be analyzed in the plant fragment.
Abstract: Previous research with the scanning electron microscope (SEM)-energy dispersive X-ray analyzer (EDXRA) and the electron microprobe analyzer (EMA), showed that the detection of light elements in thin sections of soils was problematic or even impossible. Consequently initial experiments were performed with the ion microprobe mass analyzer (IMMA). These preliminary investigations were carried out on a piece of root material in soil (containing both light and heavy elements) which has a 'clayey' appearance and is known as a clayified root (Parfenova et al., 1964). The presence of heavier elements in this sample was investigated by SEM-EDXRA prior to IMMA analysis. The results with the ion microprobe mass analyzer showed that all chemical elements could be analyzed in the plant fragment. Also much higher elemental detection sensitivities were found with IMMA as compared to SEM-EDXRA and EMA. This even allowed ion imaging of trace elements. High-quality ion images of both light and heavy elements could be obtained in much shorter exposure times than with SEM-EDXRA and EMA techniques. Furthermore by analysis of fragmentation ('fingerprint') spectra additional information was obtained with respect to the chemical binding of the analyzed elements. Due to these preliminary results IMMA offers full possibilities for microchemical analysis in situ of all important elements in soil specimens. This technique considerably increases possibilities in soil micromorphology. (Abstract retrieved from CAB Abstracts by CABI’s permission)

9 citations

Journal ArticleDOI
TL;DR: Pheromones interact with binding and catabolic proteins in insect olfactory sensilla, and the activated dendritic receptors are important in the transduction of a chemical binding event into an electrical signal.
Abstract: Pheromones interact with binding and catabolic proteins in insect olfactory sensilla, and the activated dendritic receptors are important in the transduction of a chemical binding event into an electrical signal. Selected results will be presented in which high specific activity tritium-labeled pheromones and pheromone analogs are synthesized and used to study proteins from insect antennae which bind and degrade pheromone molecules.

9 citations


Network Information
Related Topics (5)
Oxide
213.4K papers, 3.6M citations
83% related
Aqueous solution
189.5K papers, 3.4M citations
83% related
Adsorption
226.4K papers, 5.9M citations
82% related
Carbon nanotube
109K papers, 3.6M citations
82% related
Raman spectroscopy
122.6K papers, 2.8M citations
81% related
Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20223
202178
202076
201989
201866
201769