III–V compound semiconductors

Dean, P. J.

doi:10.1007/3540081275_3

Cited by 10 publications

(2 citation statements)

References 161 publications

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“…Our bulk GaP exhibits a relatively sharp PL peak at around 2.21 eV and weak peaks at around 2.16 and 2.11 eV, and also a broad peak at around 1.9 eV. The PL spectra of bulk GaP crystals have been studied extensively [16,17]. Referring to the literature, the peak at around 2.21 eV and those at around 2.16 and 2.11 eV seem to be due to a shallow-donor-acceptor transition and its optical phonon replica.…”

Section: Resultsmentioning

confidence: 99%

A photoluminescence study of nitrogen doping of gas-evaporated GaP microcrystals

Kim

Hayashi

Yamamoto

1996

J. Phys.: Condens. Matter

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In an attempt to produce GaP microcrystals doped with N atoms, gas evaporation was performed for a gas mixture composed of Ar and . The microcrystals exhibited photoluminescence bands characteristic of N isoelectronic traps, thereby giving clear evidence of N doping. It was found that the doping level can be controlled by varying the partial pressure of gas. The PN molecules produced near a tungsten heater seem to play an important role in the doping process.

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Section: Resultsmentioning

confidence: 99%

A photoluminescence study of nitrogen doping of gas-evaporated GaP microcrystals

Kim

Hayashi

Yamamoto

1996

J. Phys.: Condens. Matter

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“…These parasites then mature over the next 6 weeks into egg-laying adult worms. Schistosomula are susceptible to immune killing in vitro for the first 24-48 h after transformation, and then they become resistant [2][3][4][5][6]. Loss of critical surface antigens of the parasite is thought to contribute to this immune evasion [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni

Wiest¹,

Tisdale

Roberts

et al. 1988

Biochemical Journal

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Biosynthetic labelling experiments with cercariae and schistosomula of the multicellular parasitic trematode Schistosoma mansoni were performed to determine whether [3H]palmitate or [3H]ethanolamine was incorporated into proteins. Parasites incorporated [3H]palmitate into numerous proteins, as judged by SDS/polyacrylamide-gel electrophoresis and fluorography. The radiolabel was resistant to extraction with chloroform, but sensitive to alkaline hydrolysis, indicating the presence of an ester bond. Further investigation of the major 22 kDa [3H]palmitate-labelled species showed that the label could be recovered in a Pronase fragment which bound detergent and had an apparent molecular mass of 1200 Da as determined by gel filtration on Sephadex LH-20. Schistosomula incubated with [3H]ethanolamine for up to 24 h incorporated this precursor into several proteins; labelled Pronase fragments recovered from the three most intensely labelled proteins were hydrophilic and had a molecular mass of approx. 200 Da. Furthermore, reductive methylation of such fragments showed that the [3H]ethanolamine bears a free amino group, indicating the lack of an amide linkage. We also evaluated the effect of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: [3H]palmitate-labelled proteins of schistosomula and surface-iodinated proteins were resistant to hydrolysis with this enzyme. In conclusion, [3H]palmitate and [3H]ethanolamine are incorporated into distinct proteins of cercariae and schistosomula which do not bear glycophospholipid anchors. The [3H]ethanolamine-labelled proteins represent a novel variety of protein modification.

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