Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Optical Rotatory Dispersion”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 667 records · Page 37Linked to original sources

The composition and optical rotary dispersion of bovine aqueous humor.

The concentration of over 20 biochemicals in bovine aqueous humor was determined by conventional means, and the contribution of each to the observed optical rotation was estimated. Of those studied, only glucose and the total proteins made a significant contribution. However, other unidentified chemicals apparently also contribute to the optical activity since it was not possible to reconstruct the actual aqueous humor optical rotation based on the chemicals included. Alternative experimental approaches that may yield more complete results are discussed. With further work, optical rotation might be used as the basis of a noninvasive sensor for measuring the glucose concentration of aqueous humor in the intact eye.

Animals↗

[Effect of pH on the conformation properties and enzyme activity of alpha-amylase from Aspergillus terricola].

The effect of pH values on the conformation state of the protein globule and enzyme activity of alpha-amylase isolated from the culture liquid of the fungus Aspergillus terricola was studied. By the method of dispersion of optical rotation, it was demonstrated that together with the disordered structure the alpha-amylase macromolecule in its native form contained alpha-helix and beta-structures. With a pH change the enzyme macromolecule showed two conformational transformations: with a pH decrease from 4.0 to 2.0 alpha-helix uncoiled, and with a pH increase from 8.0 to 12.0 beta-form degraded. Hydrolytic activity of alpha-amylase was found to vary symbatically with the specific optic rotation in the above pH range.

Amylases↗

The helical content of zein, a water insoluble protein, in non-aqueous solvents.

The conformation of zein, a seed protein from corn, was determined by optical rotary dispersion measurements in a wide variety of nonaqueous solvents. Over a wide range of dielectric constants, in pure and mixed solvent systems, the helical content was independent of dielectric constant. Determination of the helical content of insulin and ribonuclease in several of these solvents indicated a variation in secondary structure comparable of that of zein. Though virtually insoluble in water, zein not only is a globular protein in nonaqueous solutions, but has conformational properites characteristic of more conventionally behaving globular proteins.

Acetamides↗

Change in the structure of Shope papilloma virus-induced arginase associated with mutation of the virus.

The change in the state of the virus-induced enzyme associated with a mutation in the virus provides additional evidence that the enzyme is synthesized from virus rather than rabbit genetic information. This change in structure results in differences in stability of polymerization, degree of optical rotary dispersion (ORD) specific rotation, change in elution characteristics from carboxymethyl cellulose, and a reduction in specific activity of the arginase. Liver arginase differs markedly in ORD characteristics from the virus-induced enzyme. In contrast to the virus-induced enzyme, it showed no negative Cotton effect at 233 nm until it was activated with manganese. Manganese had no influence on the ORD spectrum of virus-induced arginase. In addition, liver arginase is denatured by 4 M urea, while the virus-induced enzyme requires 10 M urea for denaturation.

Amino Acids↗

The effect of urea and guanidinium chloride on activity of subtilisin Carlsberg.

As shown by viscosity and optical rotation dispersion measurements, subtilisin Carlsberg is not denatured in the presence of 10 M urea or 6 M guanidinium chloride. This unusual structural stability made it possible to investigate the effects of these hydrophobic-bond breaking solutes on various aspects of the enzymic interaction with substrates and inhibitors. The binding of the competitive inhibitor N-benzoylarginine was decreased by urea or guanidinium chloride. The nature of this effect was such as to implicate hydrophobic interaction as making a major contribution to the binding. By contrast, Ks for the substrates N-acetyltyrosine ethyl ester, N-benzoylarginine ethyl ester and N-trans-cinnamoylimidazole was apparently unchanged by the presence of urea or guanidinium chloride. The influence of these solutes on kcat for the substrates was rather involved. Tentative hypotheses are put forward to account for the effects seen.

Arginine↗

Global and local dispersion of ventricular repolarization: endocardial monophasic action potential mapping in swine and humans by using an electro-anatomical mapping system.

This article evaluates whether the global dispersion of ventricular repolarization (DVR) can be estimated from measurements between a few adjacent or remote sites. Monophasic action potentials (MAP) were recorded from 61 +/- 18 left (LV) or right ventricular (RV) sites in 10 pigs and 44 +/- 16 LV, or RV sites in 8 patients by using the CARTO mapping system. MAP duration (MAPd) and end-of-repolarization time were calculated at each site and 13 repolarization maps from pigs and 10 from patients were reconstructed. Global dispersions in MAPd and EOR over the LV or RV were compared with the adjacent DVR among 3 - 7 MAPs in areas > or = 0.7 and < or = 1 cm(2) and with the remote DVRs between 2 MAPs with the greatest activation time difference (remote DVR1) and between the apical and laterobasal LV or RV (remote DVR2). The adjacent dispersions in end-of-repolarization and MAPd were significantly smaller than the global ones, 13 +/- 3 and 12 +/- 3 ms vs. 44 +/- 9 and 42 +/- 12 ms in pigs and 13 +/- 7 and 14 +/- 8 ms vs. 72 +/- 24 and 66 +/- 22 ms in patients. The remote DVR1 (30 +/- 8 and 17 +/- 10 ms in pigs and 40 +/- 28 and 28 +/- 17 ms in patients) and remote DVR2 (16 +/- 7 and 11 +/- 10 ms in pigs and 35 +/- 24 and 21 +/- 21 ms in patients) were also significantly smaller than the global DVRs. In conclusion, global DVR is poorly estimated from MAP recordings from a few adjacent or remote sites, suggesting the importance of obtaining global information in evaluating DVR.

Action Potentials↗

Effects of various antiplaque agents on fructosyltransferase activity in solution and immobilized onto hydroxyapatite.

Fructosyltransferases (FTFs) are extracellular enzymes which synthesize fructans from sucrose. Cell free FTFs are found in the dental plaque biofilm as well as in saliva. Fructans play an important role in the progression of dental caries, mainly by serving as an extracellular nutrition reservoir for bacteria. The objective of the present study was to compare the effects of several antiplaque agents on the synthesis of fructans by FTF immobilized on hydroxyapatite (HA) or in solution. The effect of chlorhexidine, cetylpyridinium chloride, sodium lauryl sulfate and Tween on FTF activity was tested using radioactive assays. Their effect on fructan structure was tested using circular dichrosim-optical rotative dispersion (CD-ORD) analysis and Fourier transform infrared (FT-IR) spectroscopy. Our results show that the antiplaque agents tested had an inhibitory effect on FTF activity both in the immobilized phase and in solution, although the inhibitory effect was more pronounced in solution. Structural changes in fructans, due to the presence of the antiplque agents, were recorded as additional C-H or O-H bands demonstrated in FT-IR analysis. However, non-significant changes in peak location were detected in CD-ORD spectrum between fructans synthesized in solution and on HA surfaces, and after treatment with the different antiplaque agents. Our study shows that several antiplaque agents may affect FTF activity and the synthesis of fructans by FTF, immobilized on hydroxyapatite or in solution.

Adsorption↗

[Optical rotary dispersion of some heptaene antibiotics].

Experimental differences in the curves of the optic rotation dispersion (ORD) of cystrans-heptaenic antibiotics were found. The ORD curves of amphotericin B, mycoheptin, levorin components and isolevorin A2, components of criptomycin and candidin were registered. The curves of the ORD which were smooth had been prepared in dimethylsulphoxide in the spectral range at 450 to 600 nm. In the spectral range at 300 to 420 nm the ORD curves appeared to be anomal with a complex Kotton effect, they were prepared in methyl alcohol. The Kotton effect was probably due to asymmetry of the electron membranes of polyenic chromophore induced by the other part of the polyen molecule. This was evident from the fact that the curve of the Kotton effect was situated in the same spectral range as the absorption bond of the polyenic chromophore. The oscillating structure in the absorption spectrum and the curve of the complex Kotton effect were analogous.

Amphotericin B↗

Biological significance of helical conformation of acid polysaccharides.

Optical rotary dispersion spectra have been studied of methylene blue complexes of glycosaminoglycans and different derivates of chondroitin 4-sulphate (free and protein bound complexes of different molecular weights and degrees of sulphation). Structural requirements of Ch-4S induction of the extrinsic Cotton effect in methylene blue were formulated. This Cotton effect is supposed to reflect the right-handed helical structure of the polysaccharide molecules. Ch-4S displayed induced Cotton effect both in free and in protein bound form; molecular weight should exceed 2-3000 (at least 4-6 disaccharide units), degree of sulphation should exceed 3% sulphate-sulphur content (more than 0.5 sulphate per one disaccharide unit). For comparison the effect of different derivatives of Ch-4S on the rate of in vitro collagen fibril formation was investigated. Close correlation was found between the macrostructural characteristics and the possible biological effect of Ch-4S. The biological significance of the macrostructural properties of Ch-4S is discussed.

Chondroitin↗