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1.
J Phys Condens Matter ; 27(26): 265301, 2015 Jul 08.
Article in English | MEDLINE | ID: mdl-26053470

ABSTRACT

We predict a new two-dimensional allotrope of phosphorus, which we call red phosphorene, by restructuring the segments of the previously proposed blue and black phosphorenes. Its atomic and electronic structures as well as the thermodynamic and dynamic stabilities are systematically studied by first-principles calculations. The results indicate that the red phosphorene is dynamically stable and possesses remarkably thermodynamical stability comparable to that of the black one. Because of the sp(3)-hybridization and the formation of a localized lone pair, red phosphorene is a semiconductor with an indirect band gap of about 1.96 eV, which can be effectively modulated by in-plane strains due to its wave-like configuration. We find that the red, black and blue phosphorenes show evident distinction in their layer thicknesses, surface work functions, and possible colors, based on which one can distinguish them in future experiments.

2.
J Phys Chem B ; 114(4): 1648-51, 2010 Feb 04.
Article in English | MEDLINE | ID: mdl-20055382

ABSTRACT

An analytical form connecting the energy shift of Raman modes directly to the bonding identities (order, nature, length, energy) of a specimen and the response of the bonding identities to the applied stimuli of temperature and pressure was presented for a deeper understanding of the atomistic origin of the ZnO Raman shift. Theoretical reproduction based on the BOLS correlation theory [Sun, C. Q. Prog. Solid State Chem. 2007, 35, 1] and the local bond average (LBA) approach [Sun, C. Q. Prog. Mater. Sci. 2009, 54, 179] of the measurements revealed that the thermally softened ZnO Raman modes arise from bond expansion and bond weakening due to vibration and that the pressure-stiffened Raman modes result from bond compression and bond strengthening due to mechanical work hardening. The developed approach could be useful in generalizing the lattice dynamics directly to the process of vibration and relaxation of a representative bond of the specimen under external stimuli.

3.
Sci China B ; 35(4): 429-36, 1992 Apr.
Article in English | MEDLINE | ID: mdl-1590918

ABSTRACT

The effects of reduction by DTT, oxidation by DTNB and treatment with NEM on the thiol contents and insulin binding to its receptor in mice liver membranes were studied. Reduction with DTT leads to a parallel increase in the thiol content and the specific binding of insulin to the membrane. Scatchard analysis of the results shows little change in the number of binding sites but a twofold increase of the binding constant. Washing the membrane with bound insulin by a DTT containing buffer results in a more marked increase in the release of bound insulin than washing with buffer alone, suggesting that part of the insulin is bound to its receptor by covalent disulfide linkages through a thiol-disulfide exchange reaction and reduction with DTT leads to a marked increase in this "disulfide-linked" insulin. Treatment with DTNB or NEM of the DTT-reduced membrane seems to reverse the effect of DTT reduction, although the reaction of the untreated membrane with DTNB or NEM had little or no effect on the specific binding of insulin. It is suggested that initially, part of the thiols responsible for the exchange reaction may not be available for reaction with DTNB and reduction with DTT generates further thiols leading to increased specific binding in general and increased insulin binding to the receptor through covalent disulfide linkages in particular.


Subject(s)
Dithiothreitol/pharmacology , Insulin/metabolism , Receptor, Insulin/metabolism , Animals , Binding Sites/drug effects , Dithionitrobenzoic Acid/pharmacology , Ethylmaleimide/pharmacology , Liver/metabolism , Mice
4.
Zhonghua Zhong Liu Za Zhi ; 10(1): 15-8, 1988 Jan.
Article in Chinese | MEDLINE | ID: mdl-2843330

ABSTRACT

Cytotoxic effects of allyl trisulfide (Alt, a synthetic chemical identical with one of the main active principles of garlic), 5 FU, MMC and DDP on SGC 7901 ( a moderately differentiated human gastric adenocarcinoma cell line) and MGC 803 (a poorly differentiated human gastric mucoadenocarcinoma cell line) had been reported before. In this paper, effects of repeated two doses of each drug and the combination of two drugs on these two cell lines were studied using relative clone-survival test. The inhibitory effects of Alt, MMC alone or combined on MGC tumor in nude mice were observed. No drug resistance was found when any one of the four agents at the same concentration were repeated twice separately at 60 hour interval in vitro. The cytotoxic effect of the repeated two doses was approximately equal to that of the single dose at double concentration. The in vitro test of combinations of two drugs showed that Alt plus MMC or 5 FU plus DDP had markedly synergistic effect on MGC cells; 5 FU plus DDP had markedly synergistic effect on SGC cells. The inhibition test on the growth of MGC tumor in nude mice indicated that the inhibition rates of Alt, MMC alone or combined were 58.3%, 86.3% and 84.3%. The systemic toxic effect of MMC alone was severe, whereas Alt alone or MMC plus Alt showed mild toxicity. For this reason, Alt plus MMC is recommended for clinical trials on poorly differentiated gastric cancer. In addition, for the comparison of in vitro test dose and clinical dose of each drug, the principle of clinical adult dose range (CADR) is proposed.


Subject(s)
Adenocarcinoma, Mucinous/pathology , Adenocarcinoma/pathology , Allyl Compounds/pharmacology , Antibiotics, Antineoplastic/pharmacology , Garlic , Plants, Medicinal , Stomach Neoplasms/pathology , Sulfides/pharmacology , Animals , Cell Line , Cisplatin/pharmacology , Drug Screening Assays, Antitumor , Drug Synergism , Fluorouracil/pharmacology , Humans , Mice , Mitomycin , Mitomycins/pharmacology , Neoplasm Transplantation , Tumor Cells, Cultured
5.
Zhonghua Zhong Liu Za Zhi ; 9(2): 112-4, 1987 Mar.
Article in Chinese | MEDLINE | ID: mdl-3652912

ABSTRACT

This paper presents the establishment of a human pulmonary adenocarcinoma cell line Lu-YePa and its biological characteristics. The primary cells of Lu-YePa cell line were derived from a twenty six year old patient with poorly differentiated adenocarcinoma of the lung. After 36 days' culture, transfer was made and the cells proliferated steadily and rapidly afterwards. The doubling time was 34.6 hours. Mitotic index reached 49.5% on day 5. Chromosome number was subtriploid with the mode of 62. The large submetacentric marker chromosome was presented in 68% of cells. PAS positive granules were found in the cytoplasm. The study of concanavalin A condensation, electron microscopic observation, heterotransplantation and plating efficiency indicates that Lu-YePa cells are concordant with the human pulmonary adenocarcinoma cells in morphology and biological behavior.


Subject(s)
Adenocarcinoma/pathology , Lung Neoplasms/pathology , Adult , Animals , Cell Line , Humans , Male , Mice , Rats , Rats, Inbred Strains
6.
Biochim Biophys Acta ; 911(1): 19-24, 1987 Jan 05.
Article in English | MEDLINE | ID: mdl-3790596

ABSTRACT

Changes in intrinsic protein fluorescence of lobster muscle D-glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12) have been compared with inactivation of the enzyme during denaturation in guanidine solutions. The holoenzyme is completely inactivated at guanidine concentrations less than 0.5 M and this is accompanied by a red shift of the emission maximum at 335 nm and a marked decrease in intensity of the intrinsic fluorescence. At 0.5 M guanidine, the inactivation is a slow process, with a first-order rate constant of 2.4 X 10(-3) s-1. A further red shift in the emission maximum and a decrease in intensity occur at guanidine concentrations higher than 1.5 M. The emission peak at 410 nm of the fluorescent NAD derivative introduced at the active site of this enzyme (Tsou, C.L. et al. (1983) Biochem. Soc. Trans. 11, 425-429) shows both a red shift and a marked decrease in intensity at the same guanidine concentration required to bring about the inactivation and the initial changes in the intrinsic fluorescence of the holoenzyme. It appears that treatment by low guanidine concentrations leads to both complete inactivation and perturbation of the active site conformation and that a tryptophan residue is situated at or near the active site.


Subject(s)
Glyceraldehyde-3-Phosphate Dehydrogenases/antagonists & inhibitors , Guanidines/pharmacology , Animals , Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism , Guanidine , Kinetics , Muscles/enzymology , NAD/metabolism , Nephropidae/enzymology , Osmolar Concentration , Protein Conformation , Protein Denaturation , Solutions , Spectrometry, Fluorescence
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