RESUMEN
A subcritical Hopf bifurcation is prepared in a multisection semiconductor laser. In the free-running state, hysteresis is absent due to noise-induced escape processes. The missing branches are recovered by stabilizing them against noise through application of phase-sensitive noninvasive delayed optical feedback control. The same type of control is successfully used to stabilize the unstable pulsations born in the Hopf bifurcation. This experimental finding represents an optical counterexample to the so-called odd-number limitation of delayed feedback control. However, as a leftover of the limitation, the domains of control are extremely small.
RESUMEN
We demonstrate experimentally control of a chaotic system on time scales much shorter than in any previous study. Combining a multisection laser with an external Fabry-Perot etalon, the chaotic output transforms into a regular intensity self-pulsation with a frequency in the 10-GHz range. The control is noninvasive as the feedback from the etalon is minimum when the target state is reached. The optical phase is identified as a crucial control parameter. Numerical simulations agree well with the experimental data and uncover global control properties.
RESUMEN
All-optical noninvasive control of a multisection semiconductor laser by means of time-delayed feedback from an external Fabry-Perot cavity is realized experimentally. A theoretical analysis, in both a generic model as well as a device-specific simulation, points out the role of the optical phase. Using phase-dependent feedback we demonstrate stabilization of the continuous-wave laser output and noninvasive suppression of intensity pulsations.
RESUMEN
The spinach pullulanase gene was cloned and sequenced using peptide sequences of the purified enzyme as a starting point and employing PCR techniques and cDNA library screening. Its open reading frame codes for a protein of 964 amino acids which represents a precursor of the pullulanase. The N-terminal transit peptide consists of 65 amino acids, and the mature protein, comprising 899 amino acids, has a calculated molecular mass of 99kDa. Pullulanase is a member of the alpha-amylase family. In addition to a characteristic catalytic (beta/alpha)8-barrel domain, it contains a domain, F, that is specific for branching and debranching enzymes. Pullulanase cDNA was expressed in Escherichia coli, and the purified protein was compared with the enzyme from spinach leaves. Identity of the two proteins was confirmed in terms of catalytic properties, N-terminal amino acid sequences and molecular masses. The pullulanase produced by E. coli showed the same microheterogeneity as the spinach leaf enzyme: it could be resolved into two substrate-induced forms by electrophoresis in amylopectin-containing polyacrylamide gels, and, in the absence of substrate, into several free forms (charge isomers) by isoelectric focusing or chromatofocusing. Rechromatofocusing of single free forms resulted in the originally observed pattern of molecular forms. However, heterogeneity of the protein disappeared on isoelectric focusing under completely denaturing conditions when only one protein band was observed. Post-translational modifications such as glycosylation and phosphorylation could be excluded as potential explanations for the protein heterogeneity. Therefore the microheterogeneity of spinach leaf pullulanase results from neither genetic variation nor post-translational modifications, but is a property of the single unmodified gene product. The different interconvertible forms of the pullulanase represent protein populations of different tertiary structure of the same polypeptide.
Asunto(s)
Glicósido Hidrolasas/química , Spinacia oleracea/enzimología , Secuencia de Aminoácidos , Amilopectina/farmacología , Secuencia de Bases , Dicroismo Circular , Clonación Molecular , Escherichia coli/genética , Focalización Isoeléctrica , Isomerismo , Cinética , Datos de Secuencia Molecular , Proteínas de Plantas/química , Desnaturalización Proteica/efectos de los fármacos , Precursores de Proteínas/química , Procesamiento Proteico-Postraduccional/fisiología , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Proteínas Recombinantes/genética , Análisis de Secuencia de ADN , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Urea/farmacologíaRESUMEN
Concurrent pulse-radiolytic generation of flavonoid aroxyl radicals and ascorbyl radicals causes a complex kinetic interplay of competing and parallel reactions. Evaluation by "kinetic modelling," that is, taking into account all possible reactions by a set of differential equations, allowed us to determine equilibria constants for the univalent steps by a novel method. From these kinetic data we were able to calculate the redox potentials for dihydroquercetin, quercetin, rutin (a quercetin 3-glycoside), kaempferol, fisetin, and luteolin. Despite the limited number of substances, two structural criteria became apparent: all substances containing the B-ring catechol group and the 2,3-double bond have a higher redox potential than ascorbate and are consequently able to oxidize it to the ascorbyl radical. With fisetin and kaempferol having values very similar to ascorbate, only the flavanone dihydro-quercetin was capable of reducing the ascorbyl radical, thus fulfilling the so-called "ascorbate-protective" function, originally proposed by Szent-Györgyi. While flavonoids are effective radical scavengers, these rather high redox potentials for most flavonols may explain their occasional prooxidative behavior.