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PubMedDate not supplied

[Optical rotatory dispersion by 5 viruses of the tobacco mosaic virus group and their components].

Optical rotatory dispersion (ORD) spectra in 250 to 350 nm region were measured for preparations of five TMV-like viruses (TMV vulgare, HR and U2 strains of TMV dolihosenation mosaic virus and cucumber virus 4) and also for RNA and protein preparations of these viruses. The data obtained testify against the possibility that the double peak with maxima at 286 and 293 nm observed in ORD of all the five viruses is due to interaction of tryptophan residues in virus coat protein with the RNA of the virul particle. The spectra of intravirus RNA of the five viruses, calculated as the difference between ORD of the intact virus and of its coat protein, were found to differ significantly from each other and from ORD of free RNA. ORD spectra of hybrid viruses, reconstituted from RNA of one virus and coat protein of another, proved to be identical to the ORD of the virus, whose protein was used in reconstitution. We suppose that the difference in ORD of the intravirus RNA of the five viruses reflect differences of RNA-protein interactions in them.

Chemical Phenomena↗
PubMed1976

Dependence of magneto-optical rotatory dispersion and magnetic circular dichroism of deoxy- and methemoglobin on their quaternary structure.

Methods of magnetic optical activity, magneto-optical rotatory dispersion (MORD) and magnetic circular dichroism (MCD), were shown to be sensitivie to the quaternary structure of deoxyhemoglobin. The isolated alpha and beta chains, the monomeric hemoglobins (leghemoglobin, fraction III of Chironomus thummi thummi hemoglobin) and hemoglobin in the R state (hemoglobin digested with carboxypeptidases A and B) exhibit in the visible region two MORD minima of equal intensities. In native tetrameric hemoglobins studied (human, horse, porcine, feline, carp, tortoise, frog) the ratio of the intensities of these MORD minima is about 2. The MORD data for deoxy-des Arg-N-ethylsuccinimide-hemoglobin indicate that in solution there is a mixture of the T and R states, the equilibrium between the states being shifted toward the R structure. The identity of the MORD curves for deoxy-bis(N-maleimidoethyl)-ester-hemoglobin and for native deoxyhemoglobin indicates that deoxy-bis(N-maleimidoethyl)ester-hemoglobin has the T structure in solution. Comparison of the MORD curves exhibited by a native methemoglobin, a native metmyoglobin and the modified hemoglobins in the met form in the absence and presence of organic and inorganic phosphates reveals no direct correlation between the MORD changes and methemoglobin quaternary structure.

Binding Sites↗
PubMed1977

[Optical rotatory dispersion of levorin and isolevorin].

Optical rotation dispersion of levorin A2 and isolevorin A2, macrocyclic heptaen antibiotics in the region of 260--320 nm due to the presence of ketogroups in the molecules of these antibiotics was studied. On the basis of the study of the optical rotation dispersion, diffusion properties and molecular models of the antibiotics it was supposed that levorin and isolevorin differed in the space configuration of the macrocycli lactone ring.

Antifungal Agents↗
PubMed1977

Circular dichroism, optical rotatory dispersion, and absorption studies on the conformation of bovine rhodopsin iw situ and solubilized with detergent.

Circular dichroism, optical rotatory dispersion and absorption of rhodopsin, the visual pigment of bovine rod outer segment membranes, were studied in situ and in membranes solubilized with various detergents. The alpha-helical content of the membrane protein is approximately 30%. The membrane protein possesses little beta-structure. Solubilization of the membrane by the detergents, Emulphogene BC-720 and cetyltrimethylammonium salts, results in loss of protein helical structure and perturbation of aromatic residues. These effects are not observed on digitonin solubilization. In regard to the structural stability of the membrane during bleaching, the following conclusions were reached: (1) Delocalized conformational changes of rhodopsin in situ involving secondary and/or tertiary structure are very unlikely. (2) Localized conformational changes of rhodopsin in situ involving secondary structure must be limited to the involvement of no more than three amino acid residues and localized conformational changes involving tertiary structure must be limited to very short segments of the protein chain containing, at the most, only a few aromatic residues. (3) Large changes in the interaction of lipid and protein moieties of the membrane are unlikely. (4) The detergents, Emulphogene, cetyltrimethylammonium salts, and digitonin, significantly decrease the conformational stability of rhodopsin as compared to the in situ conditions. The effect is smaller with digitonin. Evidence is presented against a proposed mechanism by which optical activity of the prosthetic group, retinal, is induced by resonance coupling of the transition dipoles of retinal and the lowest energy transitions of the aromatic groups of the apoprotein, opsin. A mechanism in which atropisomers of retinal are preferentially bound by opsin is consistent with the present results. The optical activity of the prosthetic group is markedly changed upon solubilization of the membrane by detergent. This change in optical activity is probably coupled to changes in conformation of the protein moiety induced by solubilization.

Animals↗
PubMed1976

[Quantitative analysis of absorption spectra and spectra of magneto-optical rotatory dispersion of hemoproteins with reference to zero-field splitting. I. Analysis of the divalentcation of deuteroporphyrin in the Q-band region].

I. Analysis of the dication of deuteroporphyrin in the Q-band region. Methods for quantitative analysis of absorption spectra and magneto-optical rotatory dispersion with regard to zero-field splitting of a nearly degenerated term for the latter are described. The methods are based on adaptation of band-form functions to the spectrum using the principle of least squares. Calculation of the zero-field splitting utilizes the formalism evolved by Stephens for strictly degenerated terms (A-terms in the magneto-optical spectrum) which has been further developed to a band-form function depending on zero-field splitting. The curve-form function of the modified A-term contains 4 parameters (zero-field splitting, rotational strength, band width, and the maximum of the band) which have been determined by a computer program. The oscillator and the dipole strength of absorption bands to be calculated simultaneously with the program allows the determination of the magnetic orbital moments of the terms. Exemplified by the dication of deuteroporphyrindimethylester, the significance of zero-field splitting for the recognition of the exact molecule symmetry is demonstrated, and a model of the molecular structure is proposed.

Cations, Divalent↗
PubMed1975

[Change in the optical rotatory dispersion characteristics of serum albumin of patients with appendicitis and cholecystitis].

The authors studied the optic rotation dispersion of serum albumin in patients suffering from cholecystitis and acute appendicitis. Conforming changes in these forms of pathology characterized by despiralization processes were established. A method of purification of albumin from its modified forms, possibly causing the mentioned changes in the albumin structure is suggested.

Acute Disease↗
PubMedDate not supplied

[Optical rotatory dispersion and circular dichroism of enzyme- and alkali-dissolved collagen].

Viscosity, dispersion of optical rotation and circular dichroism of collagen solutions was determined. Collagen solutions were obtained after treating collagen with enzymes--protorizine or prototerrizine, or with the mixture of 2,5 M NaOH--1 M Na2SO4 and acid-soluble collagen from calf skin. Molecules of "forcedly" solved collagen have an asymmetric shape with a conformation of a three-helical helix. After being heated the latter undergoes the transformation helix-coil similar to tropocollagen molecules.

Aspergillus↗
PubMed1976

Stereochemistry of the reaction of sheep liver threonine dehydratase. A nuclear magnetic resonance and optical rotatory dispersion study of its reaction pathway and products.

Products, substrates, and inhibitors of the threonine dehydratase from sheep liver (EC 4.2.1.16) have been investigated by proton nuclear magnetic resonance and optical rotation. The alpha-ketobutyrates produced from L-threonine and L-allothreonine in 2H2O have been shown to incorporate a single deuterium into the beta position. The dehydratase forms R-alpha-ketobutyrate-beta-d from L-threonine and L-allothreonine. The alpha protons of the substrates, threonine and allothreonine, do not exchange in the presence of the dehydratase. In the presence of dehydratase, the competitive inhibitors L-cysteine and L-alanine undergo alpha-proton exchange. Highly purified dehydratase has been used to determine kinetic parameters for the usbstrates L-threonine, L-allothreonine, L-serine, and L-chloroalanine. L-Chloroalanine, in addition to being a substrate, inhibits the dehydratase in a manner kinetically identical with that of L-serine.

Alanine↗
PubMed1976

Complexes of poly(adenylic acid) with complementary monomers.

The interaction of a number of potentially complementary monomers with poly(A) has been investigated by equilibrium dialysis, optical rotatory dispersion and ultraviolet absorption measurements. Experiments were conducted at pH 7.0, 0.15 M Na+, where poly(A) exists as a random coil with some degree of base-stacking, and at pH 6.0, 0.15 M Na+, where poly(A) adopts the protonated double-helical acid form structure below 15 degrees C. Binding isotherms show that, at 3.5 degrees C, poly(A) forms a 1 : 1 complex with xanthine at pH 6, and a 2:1 complex at pH 7, while oxoformycin forms a 1:1 complex with poly(A) at both pH 6 and pH 7. Poly(A) forms a complex, tentatively assigned 1:1 stoichiometry, with 8-azaxanthine at pH 6, but no complexing occurs at pH 7. The complexes have been characterized by their optical rotatory dispersion and ultraviolet spectra, their thermal stabilities, and their rates of formation at low temperature. All the complexes are laevorotatory at long wavelengths (greater than 300 nm) and unplex formation at low temperature is a slow process requiring many hours for completion. The complexes of poly(A) with 3-methylxanthine have been reinvestigated and shown to undergo normal helix-coil transitions; the anomalous melting behaviour noted previously [Biopolymers, 10, 21 -- 33 (1971)] has been explained. From a comparison of optical rotatory dispersion spectra, it is concluded that the poly(A) with 3-methylxanthine have similar structures, which are quite different from the structures of the corresponding complexes with 7-methylxanthine. The structures and properties of the poly(A) - monomer complexes are discussed, and compared with those of other polynucleotide - monomer complexes. No significant interaction was observed between poly(A) and hypoxanthine, allopurinol, 6,8-dihydroxypurine, 1-methylxanthine, 9-methylxanthine, theophylline, theobromine or 3,9-dimethylxanthine.

Anti-Bacterial Agents↗
PubMed1977

The dispersion of cholesterol with phospholipids and glycolipids.

Of the polar lipids studied (phospholipids and glycolipids), only phosphatidylcholine and sphingomyelin can disperse in water with up to 2 mol cholesterol/mol polar lipid. However, mixtures of phosphatidylethanolamine with small amounts of phosphatidylcholine and mixed lipids from mitochondria and myelin will also form sterol-rich dispersions. Steroids in which the 3beta-OH group is replaced by an oxo function do not form such steroid-rich dispersions. Electron microscopy and optical rotatory dispersion (ORD) show that sterols disperse with cerebrosides and gangliosides to form cylindrical structures with the regions around C atoms 3 and 7 of the sterol in less polar environments than those they occupy in phospholipid liposomes. It is proposed that choline-containing phospholipids facilitate entry of sterol molecules into the outer leaflet of cell surface membranes but that the phospholipid composition itself will not give rise to an asymmetric distribution of sterol in membranes with a high cholesterol content.

Cerebrosides↗
PubMed1976

Ligand-apomyoglobin interactions. Configurational adaptability of the haem-binding site.

1. The interaction of the haem-binding region of apomyoglobin with different ligands was examined by ultrafiltration, equilibrium dialysis and spectrophotometry, to study unspecific features of protein-ligand interactions such as they occur in, for example, serum albumin binding. 2. Apomyoglobin, in contrast with metmyoglobin, binds at pH 7, with a high affinity, one molecule of Bromophenol Blue, bilirubin and protoporphyrin IX, two molecules of n-dodecanoate and n-decyl sulphate and four molecules of n-dodecyl sulphate and n-tetradecyl sulphate. 3. The number of high-affinity sites and/or association constants for the alkyl sulphates are enhanced by an increase of hydrocarbon length, indicating hydrophobic interactions with the protein. 4. Measurements of the temperature-dependence of the association constants of the high-affinity sites imply that the binding processes are largely entropy-driven. 5. Binding studies in the presence of two ligands show that bilirubin plus Bromophenol Blue and dodecanoate plus Bromophenol Blue can be simultaneously bound by apomyoglobin, but with decreased affinities. By contrast, the apomyoglobin-protoporphyrin IX complex does not react with Bromophenol Blue. 6. Optical-rotatory-dispersion measurements show that the laevorotation of apomyoglobin is increased towards that of metmyglobin in the presence of haemin and protoporphyrin IX. Small changes in the optical-rotatory-dispersion spectrum of apomyoglobin are observed in the presence of the other ligands. 7. It is concluded that the binding sites on apomyoglobin probably do not pre-exist but appear to be moulded from predominantly non-polar amino acid residues by reaction with hydrophobic ligands. 8. Comparison with data in the literature indicates that apomyoglobin on a weight basis has a larger hydrophobic area avaialble for binding of ligands than has human serum albumin. On the other hand, the association constants of serum for the ligands used in this study are generally somewhat larger than those of apomyoglobin.

Apoproteins↗
PubMed1975

Isolation and partial characterization of the major proteins of rabbit sciatic nerve myelin.

The P0, P1, and P2 proteins were isolated from rabbit sciatic nerve and demonstrated to have molecular weights of 30,000, 18,200, and 12,000, respectively, by polyacrylamide disk gel electrophoresis in the presence of sodium dodecyl sulfate. The P1 protein characterized by peptide mapping, optical rotatory dispersion and encephalitogenic activity appears to be quite similar to the CNS myelin basic protein. The P2 protein is distinctly different from the P1 protein as characterized by peptide mapping and optical rotatory dispersion. It appears to have a distinct secondary structure, predominantly of beta-configuration. The P0 protein is distinctly different from either of the basic proteins, especially with respect to its marked insolubility in aqueous solutions. It contains more than 1.0 mole of hexosamine which is not present in either the P1 or P2 protein. Both the P0 and P2 proteins failed to produce any evidence of experimental allergic encephalomyelitis or neuritis when injected into guinea pigs or monkeys. In contrast, the P1 protein produces experimental allergic encephalomyelitis in both species.

Animals↗
PubMed1977

Determination of enantiomeric homogeneity (optical purity) of cyclophosphamide by nuclear magnetic resonance spectroscopy.

The enantiomeric homogeneity of resolved samples of the chiral anticancer drug cyclophosphamide was evaluated directly by 1H and 31P nuclear magnetic resonance spectroscopy with the use of the optically active shift reagent tris-[3-(trifluoromethylhydroxymethylene)-d-camphorato]europlum(III). These measurements, in concert with optical rotatory dispersion spectroscopy, established that, for optically pure cyclophosphamide, [alphaD] = 2.3 +/- 0.2 degrees.

Cyclophosphamide↗