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  • Site-directed mutagenesis  (1)
  • evanescent field  (1)
  • suppressor  (1)
  • 1
    ISSN: 1349-9432
    Schlagwort(e): waveguide ; evanescent field ; hemoglobin ; optical sensor ; thin film
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract A simple method for determining the absorption coefficient of oxyhemoglobin and deoxyhemoglobin in human blood is proposed. The method is based on a variation of the complex propagation constant of guided wave in a thin-film optical waveguide. On the waveguide layer, a serial multi-channel sample chamber is constructed to vary the interaction length between the evanescent field and the sample, and the dependence of the sensor response on the interaction length is investigated for various concentrations of two hemoglobins. The response of this sensor is linearly proportional to the interaction length and the concentration of the two hemoglobins. The attenuation constant due to the evanescent field absorption between the channels is experimentally obtained with the designed sensor, and the absorption coefficient is determined by the proposed method. The determined absorption coefficients coincided with those obtained by conventional transmission measurement.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 210 (1987), S. 413-418 
    ISSN: 1617-4623
    Schlagwort(e): Saccharomyces cerevisiae ; cAMP-dependent protein kinase ; Regulatory subunit ; Site-directed mutagenesis ; Phosphorylation site
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Four mutants with amino acid substitution(s) at or near the putative phosphorylation site (Arg142 Arg143 Thr144 Ser145) of the regulatory subunit of cAMP-dependent protein kinase were obtained by site-directed mutagenesis. Three mutants, BCY1 Ala 145 (Ser145 to Ala), BCY1 His 143 (Arg143 to His) and BCY1 Asn 144, Ala 145 (Thr144 to Asn and Ser145 to Ala) complemented a bcy1 mutant, whereas BCY1 Gly 143 (Arg143 to Gly) did not. In addition, mutant, BCY1 Asn 144, Ala 145 exhibited a dominant coldsensitive phenotype, which can be most easily explained by the functional alteration of the regulatory subunit of cAMP-dependent protein kinase by the mutations. Analyses of these mutant genes revealed that phosphorylation of the regulatory subunit is not a prerequisite for the regulation of the cAMP-dependent protein kinase activity in responding to the cAMP level.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 1 (1985), S. 25-38 
    ISSN: 0749-503X
    Schlagwort(e): Cyclic AMP ; phosphoprotein phosphatase ; protein kinase ; suppressor ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: The ppd1 mutant of yeast, Saccharomyces cerevisiae, was isolated as a suppressor of the cyr2 mutation which caused alteration of the catalytic subunit of cAMP-dependent protein kinase. Three peaks of phosphoprotein phosphatase activity (peak I, II and III) were identified by DEAE-Sephacel chromatography of crude extracts of the wild-type strain. The ppd1 mutant was deficient in peak III phosphoprotein phosphatase activity. The peak III enzyme efficiently utilized the phosphorylated forms of NAD-dependent glutamate dehydrogenase and trehalase as substrate. The ppd1 mutation did not suppress the cyr1, CYR3 or ras1 ras2 mutations. The ppd1 locus was located on chromosome II and had identical characteristcs with glc1. The ppd1 mutation suppressed the G1 arrest caused by nutritional limitation, but maintained sensitivity to mating pheromone. In diploids homozygous for the ppd1 mutation, no premeiotic DNA replication and commitment to intragenic recombination occurred and no spores were formed, suggesting that the accumulation of phosphorylated proteins in the absence of one of the phosphoprotein phosphatases is required for mitosis but not for the initiation of meiosis.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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