Active robust optimization: enhancing robustness to uncertain environments.

Many real world optimization problems involve uncertainties. A solution for such a problem is expected to be robust to these uncertainties. Commonly, robustness is attained by choosing the solution's parameters such that the solution's performance is less influenced by negative effects of the uncertain parameters' variations.

Interactive evolutionary multiobjective search and optimization of set-based concepts.

This paper deals with interactive concept-based multiobjective problems (IC-MOPs) and their solution by an evolutionary computation approach. The presented methodology is motivated by the need to support engineers during the conceptual design stage. IC-MOPs are based on a nontraditional concept-based approach to search and optimization.

Reaction of rabbit skeletal myosin with D-glucose 6-phosphate.

Incubation of rabbit skeletal myosin with 1 to 3 mM D-glucose 6-phosphate over a period of several hours resulted in the inhibition of the K(+)- and actin activated-ATPase activities. Substrate ATP (0.5-3 mM final concentration) protected the myosin against the loss of ATPase activity as induced by glucose 6-phosphate.

Isolation and partial characterization of collagen chains dimerized by sugar-derived cross-links.

Incubation of tail tendon from a young rat in solutions containing D-ribose resulted in attachment of the monosaccharide to collagen and subsequent cross-link formation at a rate much faster than found for glucose. The collagen rapidly became resistant to solubilization and showed increasing fluorescence. Ribose bound to all major CNBr peptides of collagen, with some preference for the alpha 2-CB3,5 peptide and the triple-helical region of alpha 1-CB6, and was incorporated into higher molecular weight material.

Glycation induces expansion of the molecular packing of collagen.

Exposure of rat tail tendon to a reducing sugar results in covalent attachment of the sugar to collagen, a process termed glycation, and leads to the formation of stable intermolecular cross-links. We have used X-ray diffraction to study the changes in the crystalline unit cell of rat tail tendon collagen brought about by glycation. Ribose was selected as a model compound for most of the study because its reaction with proteins is faster than that of glucose, and therefore more convenient for laboratory studies, but glucose and glyceraldehyde were used as well.

Structures of D-threo-2,5-hexodiulose 1-phosphate and D-threo-2,5-hexodiulose 1,6-bisphosphate (5-keto-D-fructose mono- and bis-phosphate) in solution by 13C-N.M.R. spectroscopy.

The mono- (2) and bis-phosphate (3) derivatives of D-threo-2,5-hexodiulose (1) (5-keto-D-fructose) were synthesized enzymically and purified by anion-exchange chromatography. The proportions, sizes of ring, and anomeric configurations were determined by F.t.

Oxidation rates of some desialylated glycoproteins by galactose oxidase.

Patterns of oxidation of dilute solutions of desialylated fetuin and submaxillary mucin by galactose oxidase have been examined. A significant portion (20-40%) of the terminal galactosyls exposed on the glycoproteins, which theoretically were expected to be accessible to the enzyme, was not oxidized. In comparison, galactosyls in oligosaccharides released from completely desialylated glycoproteins were oxidized more effectively with an apparently lower degree of crypticity to the enzyme.

A simple spectrophotometric determination of formaldehyde and other aldehydes: application to periodate-oxidized glycol systems.

A simple, rapid, and sensitive spectrophotometric assay procedure for the determination of as low as 2 microM solutions of formaldehyde and acetaldehyde using an alkaline 4-amino-5-hydrazino-3-mercapto-1,2,4-triazole reagent is described. The method is particularly useful for determination of these aldehydes (0.5-50 nmol) when produced by the periodate oxidation of various glycols and can be applied to the assay of dilute solutions of sugars or polyols.

Solution structure of 5-keto-D-fructose: relevance to the specificity of hexose kinases.

5-Keto-D-fructose (5KF) is isolated from cultures of Gluconobacter cerinus growing on D-fructose as the sole carbon source. 5KF is a substrate for hexokinase, fructokinase, and several polyol dehydrogenases. 1H and 13C nuclear magnetic resonance studies show that 5KF exists in different forms in anhydrous dimethyl-d6 sulfoxide and D2O.

A coupled NAD+-peroxidase spectrophotometric assay for cholesterol.

We describe a modified enzymic reagent for determination of cholesterol and cholesterol ester in serum and in high-density lipoprotein. In this new procedure, the hydrogen peroxide produced by the action of cholesterol oxidase is used as a substrate for NAD+ peroxidase. Spectrophotometric determination of the NADH consumed in this coupled reaction provides a direct and absolute measure of the cholesterol originally present in free form and that liberated by the action of cholesterol ester hydrolase.

Reduction of nicotinamide adenine dinucleotides by sodium cyanoborohydride.

The relatively slow reduction of NAD+ and NADP+ by sodium cyanoborohydride leads to formation of the enzymically active form of NADH and NADPH. This reaction could be useful as a simple procedure to enzymically introduce a specific label into substrates when tritiated or deuterated cynanoborohydride is used for obtaining the reduced nicotinamide adenine dinucleotide.

Dansyl hydrazine as a fluorimetric reagent for thin-layer chromatographic analysis of reducing sugars.

Reducing sugars, particularly aldoses, react readily with dansyl hydrazine. The fluorescent hydrazones produced can be separated by thin-layer chromatography and determined quantitatively by spectrofluorimetry after elution from the chromatograms.

Interactions between aerolysin, erythrocytes, and erythrocyte membranes.

Aerolysin, a hemolytic and lethal exotoxin of Aeromonas hydrophila, was analyzed for amino acids. Assuming 8 histidine residues/mol, the purified toxic protein has, by summation, a molecular weight of 49,000, a value in agreement with earlier estimates by other methods. Erythrocytes from different animal species differ greatly in sensitivity to aerolysin's lytic action.

Metabolic consequences of a block in the synthesis of 5-keto-D-fructose in a mutant of Gluconobacter cerinus.

A mutant of Gluconobacter cerinus var. ammoniacus, IFO 3267, has been isolated which is deficient with respect to fructose 5-dehydrogenase, the enzyme catalyzing the oxidation of d-fructose to 5-keto-d-fructose (5 KF). Growth of this mutant on fructose as the sole carbon source was impaired unless the culture medium was supplemented with 5 KF.

5-Keto-D-fructose: formation and utilization in the course of D-fructose as similation by Gluconabacter cerinus.

The accumulation of 5-keto-d-fructose (5KF) by Gluconobacter cerinus grown on d-fructose in unbuffered medium was shown to be optimal at pH 4.0 after cell growth ceased. During the exponential phase of growth or at neutral pH after the onset of the stationary phase, 5KF production continued but did not accumulate because of its rapid reutilization by reduction to d-fructose.