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  • Blattella germanica  (1)
  • op amps  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Analog integrated circuits and signal processing 19 (1999), S. 139-144 
    ISSN: 1573-1979
    Keywords: op amps ; comparators ; cascading ; analog ; compact ; high gain ; self-biased ; CMOS VLSIC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology
    Notes: Abstract This paper discusses the design of high gain, general purpose op amps. The op amp is based on a novel cascaded design using comparators and with structural simplicity approaching that of digital circuits. Ideally, the design tool presented here can be used to optimize gain and CMRR independent of the other op amp performance parameters. The designed op amp has 140 dB open-loop gain and 43 MHz unity gain frequency (GBW) in Berkeley Spice3f Level-2 simulation. The circuit is implemented using a 2.0 μm nwell CMOS process through MOSIS. The op amp is self-biased and requires only power supplies of ±2.5 V. It occupies an area of 113 μm×474 μm.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 237-250 
    ISSN: 0739-4462
    Keywords: yolk phosphatase ; α-mannosidase ; Blattella germanica ; proteolytic processing ; vitellin ; embryo development ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Proteolytic processing of the vitellin in Blattella germanica eggs occurs 4 days postovulation and is correlated with both the onset of its utilization and the major portion of the embryo's growth. Yolk phosphatase is also expressed coincident with this event, and some aspects of its activation have been investigated. The enzyme is absent from the ooplasm (yolk) during the first 2 days following ovulation but increases approximately 20-fold in specific activity between days 3 and 4, when assayed at pH 3.9 or 4.8 and 9-fold at pH 6.5. No activation is observed for yolk-bound α-mannosidase, its specific activity remains elevated through the first 6 days following ovulation. This suggests that expression of the phosphatase is regulated independently of that of α-mannosidase in the yolk. Yolk with active phosphatase can dephosphorylate native vitellin, delipidated vitellin, and phosphocasein. Sucrose density gradient centrifugation of yolk obtained from eggs 4 days postovulation, revealed that phosphatase activity cosediments with material which reacts with antivitellin antibodies, while α-mannosidase and β-N-acetyl glucosaminidase are found near the top of the gradient. Oothecae derived from crossing certain translocational heterozygote males and wild-type females contain some eggs with severely depressed levels of yolk phosphatase in which embryos do not grow. Vitellin in these eggs fails to undergo proteolytic processing as late as day 5 postovulation and retains the subunit composition of freshly ovulated vitellin.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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