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J R Gao

Publications and source records attributed to J R Gao.

10 recordsLinked to original sources
PubMed2006

Antenna model for wire lasers.

An antenna model is proposed for long (L >> A) lasers with subwavelength cross sections (wire lasers). It is shown that the far-field pattern of the wire lasers is determined by the ratio of the wavelength to the length. The radiation of the wire laser is predicted to be concentrated in a narrow beam theta approximately radical(2lambda/L) for laser modes where the longitudinal phase velocity is in synchronism with the velocity of light in air. Experimental results obtained using a terahertz quantum cascade wire laser are in agreement with the model.

Journal Article↗
PubMed2001

An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics.

An acetylcholinesterase (AChE, EC 3.1.1.7) was purified from the greenbug, Schizaphis graminum (Rondani). The maximum velocities (Vmax) for hydrolyzing acetylthiocholine (ATC), acetyl-(beta-methyl) thiocholine (AbetaMTC), propionylthiocholine, and S-butyrylthiocholine were 78.0, 67.0, 37.4, and 2.3 micromol/min/mg, and the Michaelis constants (Km) were 57.6, 60.6, 31.3, and 33.4 microM, respectively. More than 98% of AChE activity was inhibited by 10 microM eserine or BW284C51, but only 7% of the activity was inhibited by ethopropazine at the same concentration. Based on the substrate and inhibitor specificities, the purified enzyme appeared to be a true AChE. Nondenaturing polyacrylamide gel electrophoresis (PAGE) and isoelectric focusing of the purified AChE revealed three molecular forms. The isoelectric points were 7.3 for the major form and 6.3 and 7.1 for two minor forms. The major form of purified AChE showed molecular masses of 129 kDa for its native protein and 72 kDa for its subunits on SDS-PAGE. However, the purified AChE exhibited some distinctive characteristics including: (1) lack of affinity to the affinity ligand 3-(carboxyphenyl) ethyldimethyl ammonium, which has been used widely in purification of AChE from various insect species; and (2) 20-200-fold higher substrate-inhibition thresholds for ATC and AbetaMTC than AChE from other insect species. These biochemical properties may reflect structural differences of AChE purified from the greenbug compared with that from other insect species.

Acetylcholinesterase↗
PubMed2000

Comparative toxicity of selected organophosphate insecticides against resistant and susceptible clones of the greenbug, Schizaphis graminum (Homoptera: aphididae).

Comparative toxicity of selected organophosphate (OP) insecticides against resistant and susceptible clones of the greenbug, Schizaphis graminum, were studied both in vitro and in vivo. Two resistant (OR-1 and OR-2) clones of the greenbug showed marginal to high levels of resistance to all seven OPs tested, ranging from 11- to 327-fold greater than those of a susceptible (OSS) clone. The OR-1 clone showed lower levels of resistance to phenyl (parathion and parathion-methyl) and heterocyclic (chlorpyrifos) OPs than to aliphatic OPs (dimethoate, omethoate, disulfoton, and demeton-S-methyl), whereas the OR-2 clone showed a rather broad spectrum of resistance to nearly all OP insecticides examined. In vitro inhibition of acetylcholinesterase (AChE) using six selected OP oxon analogues showed that alterations of AChE were involved in resistance to all OP compounds examined in both the OR-1 and OR-2 clones. Although the levels of insensitivity of AChE to these OPs were relatively low, ranging from 1.1- to 3.8-fold, the insensitivity spectrum of AChE to different OPs was rather broad. The general esterase activity in the OR-1 and OR-2 clones was 1.3-8. 4-fold higher than that in the OSS clone, depending on the substrates used. The AChE activity in both the OR-1 and OR-2 clones was 1.8-fold higher than that in the OSS clone. High resistance levels of the OR-2 clone to phenyl and heterocyclic OPs appeared to be associated with the ability of the esterases to hydrolyze beta-naphthyl acetate and more hydrophobic substrates.

Acetylcholinesterase↗
PubMed1998

Purification and kinetic analysis of acetylcholinesterase from western corn rootworm, Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae).

Acetylcholinesterase (AChE, EC 3.1.1.7) was purified from western corn rootworm (WCR, Diabrotica virgifera virgifera) beetles by affinity chromatography. The purification factor reached over 20,000-fold with a specific activity of 169.5 mumol/min/mg and a yield of 23%. The Vmax values for hydrolyzing acetylthiocholine (ATC), acetyl-(beta-methyl) thiocholine (A beta MTC), propionylthiocholine (PTC), and S-butyrylthiocholine (BTC) were 184.8, 140.5, 150.2, and 18.8 mumol/min/mg, respectively, and K(m) values were 19.7, 18.5, 14.1, and 11.0 microM, respectively. The first three substrates showed significant inhibition to the AChE at higher concentrations, whereas BTC showed inhibition at the concentrations of 0.25-2 nM but activation at > 4 mM. AChE activity was almost completely inhibited by 1 microM eserine and BW284C15, respectively, but only 12% of AChE activity were inhibited by ethopropazine at the same concentration. These results suggested that the purified AChE from WCR was a typical insect AChE. Insecticides or their oxidative metabolites, chlorpyrifos-methyl oxon, carbofuran, carbaryl, malaoxon, and paraoxon, used in in vitro kinetic study exhibited high inhibition to AChE purified from WCR. However, chlorpyrifos-methyl oxon and carbofuran showed at least 36- and 4-fold, respectively, higher inhibitory potency than the remaining insecticides examined. Results from our in vitro inhibition of AChE agreed quite well with the previously published in vivo bioassay data.

Acetylcholinesterase↗
PubMed1986

Detergent, Brij, increasing the area of new surface membrane during the early cleavage of eggs of Rana amurensis.

The exposure of new surface membrane occurred in the cleavage furrow of Rana amurensis eggs enclosed in fertilization membrane immersed in Brij solution. The exposed area increased gradually and reached a maximum while the furrow extended to 240 degrees around the egg surface. At this time, the new membrane area of the treated eggs was significantly larger than that of the control. Afterwards, the exposed new membrane area decreased gradually. This may result from the extent of new membrane increase being less than the extent of contraction of cleavage furrow.

Animals↗