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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Materials research innovations 3 (1999), S. 66-68 
    ISSN: 1433-075X
    Keywords: Key words Uncooled detectors ; IR bolometers ; Ferricytochrome c layers ; High TCR ; Negative resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract  The current infrared microbolometer technology using vanadium oxide material is not quite as sensitive as a cooled platinum silicide or cooled mercury cadmium telluride or indium antimonide array. The performance factor of the present IR bolometer needs to be improved by at least an order of magnitude to make a bolometric IR device comparable to the cooled detector arrays. I recently reported [1] that thin films of globular proteins such as cytochrome c exhibit a high temperature coefficient of resistance (TCR) value of about 10% as compared with a value of 2.0 to 2.5% normally observed in VOx films. The measurements that were initially reported were taken two weeks after the thin films had been prepared. The measurement of the TCR values presented in this report were taken within three days of the films being prepared. These TCR values are very high, approximately 35% for temperatures between 25 and 60°C, and they have a sheet resistance around 1 to 2 Ω/cm2 with a current of 1 mA. The values of TCR were very uniform over the wafer surface, but the values varied slightly from wafer to wafer. It appears that a cytochrome c monolayer on metal oxide semiconductor (CMOS) electronics could generate miniaturized, uncooled IR detector arrays that would be suitable for military and commercial applications that require very high performance and low-power drain. With these high TCR values, biological uncooled devices will have the potential for long-range thermal imaging applications comparable to cooled detectors. I have also examined the sheet resistance of the protein layer with an increase in the bias current near ambient temperature. I found that the sheet resistance of cytochrome c rapidly goes towards the negative values as the bias current is increased. On the other hand, TCR characteristics remained unchanged with an increase in bias current. This is a very interesting phenomenon that has never been reported in biomolecules. I am making further explorations into the electrical properties of many proteins for possible device applications.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: heterologous expression ; introduction of positive supercoils in DNA ; Pisum sativum ; RACE-PCR ; relaxation of DNA supercoils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated and sequenced the full length cDNA for topoisomerase I. Using degenerate primers, based on the conserved amino acid sequences of five eukaryotic topoisomerase I, a 386 bp fragment was PCR amplified using pea cDNA as template. This fragment was used as a probe to screen a pea cDNA library. Two partial cDNA clones were isolated which were truncated at the 5′ end. RACE-PCR was employed to isolate the remaining portion of the gene. The total size of the gene was 3055 bp with an open reading frame of 2676 bp. The deduced structure of pea topoisomerase I contain 892 amino acids with a calculated molecular weight of 100 kDa and an estimated pI of 9.3. A comparison of the deduced amino acid sequences of the pea topo I with the other eukaryotic topoisomerases clearly suggested that they are all related. Pea topoisomerase I has been overexpressed in E. coli system and the recombinant topoisomerase purified to homogeneity. The purified protein relaxes both positive and negative supercoiled DNA in the absence of divalent cation Mg2+. In the presence of Mg2+ ions the purified enzyme introduces positive supercoils a unique property not reported in any other organism except in archaebacterial topoisomerase I. Polyclonal antibodies were raised against recombinant topoisomerase I and western blotting with sub-cellular fractions indicated the localization of this topoisomerase in pea nuclei.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5028
    Keywords: cell proliferation ; in vitro transcription and translation ; Pisum sativum ; plant promoter ; primer extension ; RACE-PCR ; transcript analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated and sequenced four overlapping cDNA clones to identify the full-length cDNA for topoisomerase II (PsTopII) from pea. Using degenerate primers, based on the conserved amino acid sequences of other eukaryotic type II topoisomerases, a 680 bp fragment was PCR-amplified with pea cDNA as template. This fragment was used as a probe to screen an oligo-dT-primed pea cDNA library. A partial cDNA clone was isolated that was truncated at the 3′ end. RACE-PCR was employed to isolate the remaining portion of the gene. The total size of PsTopII is 4639 bp with an open reading frame of 4392 bp. The deduced amino acid sequence shows a strong homology to other eukaryotic topoisomerase II (topo II) at the N-terminus end. The topo II transcript was abundant in proliferative tissues. We also show that the level of topo II transcripts could be stimulated by exogenous application of growth factors that induced proliferation in vitro cultures. Light irradiation to etiolated tissue strongly stimulated the expression of topo II. These results suggest that topo II gene expression is up-regulated in response to light and hormones and correlates with cell proliferation. Besides, we have also isolated and analysed the 5′-flanking region of the pea TopII gene. This is first report on the isolation of a putative promoter for topoisomerase II from plants.
    Type of Medium: Electronic Resource
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