RESUMO
It is crucial to control the tuning and improve the emission of a quantum emitter at the nanoscale. We report multiple Fano resonances in metallic nanostructures on an Er3+-doped tellurite glass. Periodic nanoslits were fabricated with a focused gallium ion beam on a gold thin film deposited on the tellurite glass. Is proposed a coupling function with Fano line-shape form, and the asymmetric parameter q for each resonance wavelength in the 515 to 535 nm region was calculated. This asymmetric resonance effect is a consequence of the quantum interaction between the continuum state, generated in the nanostructure, and the Stark splits of the [Formula: see text]H[Formula: see text] state.
Assuntos
Angina Instável/tratamento farmacológico , Fibrinolíticos/uso terapêutico , Heparina de Baixo Peso Molecular/uso terapêutico , Infarto do Miocárdio/tratamento farmacológico , Fibrinolíticos/economia , Heparina de Baixo Peso Molecular/economia , Humanos , Ensaios Clínicos Controlados Aleatórios como AssuntoRESUMO
The catalytic subunit of protein phosphatase-1 (PP1) isolated from rabbit liver had the same electrophoretic mobility as, and yielded peptide maps identical to those of the 33 kDa form of rabbit skeletal muscle PP1. The predicted amino-acid sequences of PP1 obtained from three rabbit liver cDNA clones were identical to that of PP1 alpha from rabbit skeletal muscle. These findings suggest that the distinctive substrate specificities and regulatory properties of hepatic and skeletal muscle type-1 protein phosphatases are not conferred by the catalytic subunits themselves, but by regulatory subunits that are complexed to the catalytic subunits in vivo.
Assuntos
Genes , Fígado/enzimologia , Músculos/enzimologia , Fosfoproteínas Fosfatases/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , Substâncias Macromoleculares , Dados de Sequência Molecular , Especificidade de Órgãos , Mapeamento de Peptídeos , Fosfoproteínas Fosfatases/isolamento & purificação , Proteína Fosfatase 1 , Coelhos , Mapeamento por RestriçãoRESUMO
A cDNA encoding a novel protein phosphatase catalytic subunit (protein phosphatase X) has been isolated from a rabbit liver library. It codes for a protein having 45% and 65% amino acid sequence identity, respectively, to the catalytic subunits of protein phosphatase 1 and protein phosphatase 2A from skeletal muscle. The enzyme is neither the hepatic form of protein phosphatase 1 or 2A, nor is it protein phosphatase 2B or 2C. The possible identity of protein phosphatase X is discussed.
Assuntos
DNA/genética , Fosfoproteínas Fosfatases/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , DNA Recombinante , Fígado/enzimologia , Dados de Sequência Molecular , Músculos/enzimologia , Hibridização de Ácido Nucleico , Proteína Fosfatase 1 , Proteína Fosfatase 2 , Coelhos , Homologia de Sequência do Ácido NucleicoRESUMO
The amino acid sequences of mammalian protein phosphatase 1 and 2A were compared pairwise with every sequence in the National Biomedical Research Foundation protein sequence database using an exhaustive searching programme [Coulson et al., Comp. J. 30 (1987) 420-424]. The N-terminal half of the protein encoded by an open reading frame, orf 221, in bacteriophage lambda (nt 43,224-43,886 in the map of Daniels et al. [in Hendrix et al. (Eds.), Lambda II. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1983, pp. 519-676] shows 35% identity to either protein phosphatase 1 or 2A in this region. If conservative replacements are included the overall homology rises to 49%. A gene in phi 80 also shows 35% identity with the mammalian protein phosphatases. The results indicate that orf 221 of phage lambda and the homologous phi 80 gene may encode protein phosphatases. The possible roles of protein phosphorylation in the propagation of bacteriophage are discussed.
Assuntos
Bacteriófago lambda/genética , Colífagos/genética , Genes Virais , Genes , Fosfoproteínas Fosfatases/genética , Sequência de Aminoácidos , Animais , Dados de Sequência Molecular , Músculos/enzimologia , Proteína Fosfatase 1 , Coelhos , Homologia de Sequência do Ácido NucleicoRESUMO
A cDNA clone encoding a second type-2A protein phosphatase catalytic subunit (2A beta) was isolated from a rabbit skeletal muscle cDNA library constructed in lambda gt10. The deduced protein sequence (309 residues, 35.59 kDa) was 97% identical to that of phosphatase 2A alpha (309 residues, 35.58 kDa). At the nucleotide level, the two clones showed only 82% identity in the coding region. The results indicate the presence of at least two isoforms of protein phosphatase 2A in skeletal muscle.
Assuntos
Músculos/enzimologia , Fosfoproteínas Fosfatases/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , DNA/isolamento & purificação , Dados de Sequência Molecular , Proteína Fosfatase 2 , CoelhosRESUMO
A 1.5 kb clone containing the full-length coding sequence of a type-1 protein phosphatase catalytic subunit has been isolated from a rabbit skeletal muscle cDNA library constructed in lambda gt10. The protein sequence deduced from the cDNA contains 311 residues and has a molecular mass of 35.4 kDa. A single mRNA species at 1.6 kb was visualized by Northern blotting. The type-1 protein phosphatase was strikingly homologous to protein phosphatase 2A, 49% of the amino acids between residues 11 and 280 being identical. The first 10 and last 31 residues were dissimilar. Residues 1-101 of the type-1 protein phosphatase also showed 21% sequence identity with a region of mammalian alkaline phosphatases.
Assuntos
Fosfoproteínas Fosfatases/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , DNA/genética , Dados de Sequência Molecular , Músculos/fisiologia , Fragmentos de Peptídeos/análise , Proteína Fosfatase 2 , RNA Mensageiro/genética , Coelhos , Homologia de Sequência do Ácido NucleicoRESUMO
A 2.5 kb clone containing the full-length coding sequence of a type-2A protein phosphatase catalytic subunit has been isolated from a rabbit skeletal muscle cDNA library constructed in lambda gt10. The sequence of the protein deduced from the cDNA contains 309 residues (35.58 kDa). A major mRNA species at 2.0 kb and a minor component at 2.8 kb were visualized by Northern blotting in both skeletal muscle and liver. The type-2A enzyme showed weak homology with mammalian alkaline phosphatases between residues 55 and 95. The protein sequence of the type-2A phosphatase from rabbit skeletal muscle differs from that reported for the bovine adrenal enzyme in three regions.
