Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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Alteration of the intermolecular interaction in aqueous solution of human serum albumin (SA) as a result of the increase of ionic strength and pH values brings about the slowing-down of the spin-echo decay curve for protein protons (several times at high SA concentrations). A specific effect of alkaline pH was observed, i.e. the slowing-down of quick component of the spin-echo decay curve. This result taken together with the data on complex spin-echo decay curve, correlation times of protons of different regions is SA and compared with SA isotope exchange data can be explained as a result of the polypeptide chain conformation mobility with frequencies more 10(4) c.p.s. This effect is observed in regions occupying about one half of the SA macromolecule volume.
Mol Biol (Mosk)
PMID:[NMR spin-echo study of behaviour dynamics of serum albumin macromolecules in aqueous solutions as a function of pH and ionic strength]. 3 29

Interaction of bovine serum albumin (BSA) with quaternized poly-4-vinyl pyridine (PE) in aqueous solutions at pH 7 was studied. It was shown that in a wide range of the ratios of the components (nBSA/nPE) soluble stable cooperative complexes were formed. At the same time a certain critical content of the protein exists at which the system loses its homogeneity. Complex formation is not accompanied by protein denaturation. At smaller nBSA/nPE ratios non-homogeneous distribution of protein globulas among polyelectrolite macromolecules was found; this corresponded to the "all or none" principle. Using ultracentrifugation technique viscosimetric measurements and electron microscopy it was shown that the soluble complexes exist in the form of rode-like particles consisting of protein globules stabilized by polycation chains. Such particle can be considered as a model of nucleoprotein complex. At certain crytical nBSA/nPE rations the rod-like particles aggregate with additional number of BSA-molecules and form more complicate soluble and insoluble cooperative complexes. Possible structural models of the complexes described were suggested and the thermodinamic and kinetic cryteria of their self-assembly were discussed.
Mol Biol (Mosk)
PMID:[Cooperative interaction of serum albumin with quaternized poly-4-vinyl pyridine and structure of the complexes]. 3 35

Immunization of animals with DNA modified by a mixture of bisulphite and O-methylhydroxylamine and methylated bovine serum albumin results in production of antibodies mainly reacting with modified DNA. Antibodies that react with denatured DNA were produced in minute quantity. It was shown that elicited antibodies possess a high specificity and have the ability to recognize only nucleotides with a double modification. The immune sera were fractionated by Sephadex G-200 column chromatography and the antibody activity was demonstrable in the 19S and 7S fractions. The attempts to induce synthesis of antibodies by injection of DNA modified by O-methylhydroxylamine failed.
Mol Biol (Mosk)
PMID:[Study of nucleic acid structure by immunochemical methods. I. Antibodies specific for 6-sulfo-5,6-dihydro-4-methoxyaminopyrimidinone-2]. 7 79

Measurement of the effect of drugs on the in vivo rates of synthesis of rabbit liver organelle bound proteins were measured following individual treatments with the inducers phenobarbital, 3-methylcholanthrene and PCB (a mixture of polychlorinated biphenyls) and the inhibitors, cycloheximide, aflatoxin B1, chloramphenicol and actinomycin D. Following their isolation from a homogenate containing the combined livers of 14C-leucine injected experimental animals and 3H-leucine injected control animals, purified fractions of the following proteins were prepared: microsomal cytochrome b5, cytochrome P-450, NADH-cytochrome b5 reductase, NADPH-cytochrome P-450 reductase and proteolipids, outer mitochondrial membrane cytochrome b5, NADH-cytochrome b5 reductase and proteolipids, inner mitochondrial membrane cytochrome c, NADH dehydrogenase and proteolipids, intermitochondrial membrane cytochrome b5 and circulating serum albumin. The effect of a drug was examined by measuring the 14C/3H ratio of leucine incorporation of each fraction; ratios which differed markedly from a control value of 1 represented actual changes in the relative rates of protein synthesis. Increased rates of synthesis of cytochrome P-450 and its reductase, intermitochondrial membrane cytochrome b5 and all three proteolipid fractions resulted from each inducer treatment. Treatments with 3-methylcholanthrene and PCB also increased the rate of synthesis of cytochrome b5 and its reductase in both the microsome and outer mitochondrial membrane. In addition, the PCB treatment increased the rates of synthesis of cytochrome c and NADH-dehydrogenase. The rates of synthesis of cytochromes, reductases and of circulating serum albumin were inhibited following treatments with cycloheximide, aflatoxin B1 and actinomycin D. Actinomycin D appeared to inhibit the release of newly synthesized albumin into the bloodstream while chloramphenicol treatment appeared to inhibit the incorporation of cytochrome c into the mitochondria. After 20 hours of treatment with inhibitors, the inhibitory effect of actinomycin D and cycloheximide were still apparent while the rates of protein synt;esis in chloramphenicol and aflatoxin B1 treated animals increased to levels above the controls. The incorporation of radioactively labeled leucine into the proteolipids of the microsomal, and the outer and inner mitochondrial membranes were inhibited following the treatment with actinomycin D and stimulated following the treatment with cycloheximide.
Mol Cell Biochem 1979 Dec 14
PMID:Effect of a single dose of inducers and inhibitors on the rate of synthesis of cytochromes and reductases in liver organelles. 11 59

A light-induced reduction of the water-soluble nitroxide radical by chlorophyll in lipid and protein--lipid micelles was demonstrated. In contrast to model systems, in whole chloroplasts the NR is photoreduced by the electrons of the noncyclic electron transport chain. The initiation of cyclic electron transport in light particles, containing only photosystem I, does not lead to photoreduction of NR. When exogenous protein -- human serum albumin -- is added to the light particles, the nitroxide radicals are intensively reduced. The specific role of protein in electron transport from P700 to the exogenous acceptor is discussed.
Mol Biol 1975 Jan
PMID:Investigation of electron transport in the chloroplasts and their fragments by the ESR method. II. Light-induced interaction of water-soluble nitroxide radical with chloroplasts and chlorophyll containing protein-lipid micelles. 16 97

To study conformational changes of protein molecules in a pre-denaturation temperature range, nitroxyl radicals adsorbed by a protein are suggested to be used. A spin probe technique is specially developed to be implied for this aim by using a probe specifically bound to the bovine serum albumin molecule, it was possible to reveal a dependence of the rotation correlation time of the adsorbed radical and the environment polarity on the temperature. The data obtained testify in favour of a change occurring in the intramolecular structure of the protein under study due to a temperature change within the pre-denaturation temperature range.
Mol Biol (Mosk)
PMID:[Study of the conformational changes of serum albumin molecules within a pre-denaturation temperature range by a spin probe technique]. 17 62

The protein spin-echo decay and recovery of longitudinal magnetization were studied in seven globular proteins: cytochrome C, ribonuclease, lysozyme, DNA, hemoglobin, serum albumin and gamma-globulin in D2O solutions. For comparison the Tobacco mosaic virus (TMV) protons in D2O solutions were also investigated. The spin-echo decay of all 7 proteins can be separated into three components: a slowly decaying component with an amplitude of about 10% of the amplitude of the total signal, intermediately and fastly decaying components, the two latter being comparable in amplitudes. Longitudinal relaxation is more simple in character. The value of T2 of the protons responsible for the fastly decaying components in linearly dependent on the molecular weight of the protein, a fact indicating that the regions of the proteins with a "rigid" structure can be responsible for this component. The intermediate component, whose contribution increases with temperature, was ascribed to the mobile regions of the protein, and the slowly decaying component to the mobile protein side chains. Weak dependence of T1 on the protein molecular weight and some other obtained data give additional evidence for the presence of motion within macromolecules. The peculiarities of this motion is in good correspondence with the notion about the existence of the segmental motion of the polypeptide chain (conformational mobility of the protein). In contrast to proteins the spin-echo decay of TMV lacked the slow component and the "solid" echo signal was observed which indicates the existence of a "rigid" structure in the macromolecules of the virus.
Mol Biol (Mosk)
PMID:[Study of the conformational mobility of globular proteins by pulse methods of NMR]. 20 75

Dependence of the rotational mobility of bovine serum albumin on the protein concentration in solution has been studied by means of nitroxyl radical tightly bound to the protein. The rotational correlation time of radical, bound with protein for weak solution has been compared with the theoretical values of correlation times for protein monomer, calculated in terms of its hydration and deviation from the spherical shape. A conclusion about radical orientation relatively to the protein molecule has been drawn from this comparison. The concentration dependence of ratational correlation time for radical, bound with protein, was explained by the protein dimerization in solution. A conclusion has been drawn about the stability of intramolecular structure of serum albumin during its dimerization on the basis of the stability of anisotropic hyperfine constants of adsorbed radical.
Mol Biol (Mosk)
PMID:[Rotatory mobility and intermolecular reactions of serum albumin studied using the spin-probe method]. 22

The rate of water proton relaxation of the solutions of human serum albumin (HSA) modified by different spin labels has been investigated by spin echo technique. The rate of proton relaxation in the presence of the labeled HSA is higher than that in water solutions of spin labels. The proton relaxation data of the protein solutions can be explained by local properties of the water, bound with the protein (in the regions of spin labels) which seem to resemble those of water-glycerol solutions. The rate of proton relaxation was decreased in the presence of steroids that can be explained by a decrease of the local microviscosity of the water-protein matrix due to interaction of steroids with HSA.
Mol Biol (Mosk)
PMID:[Interaction of steroids with human serum albumin by spin echo technique and paramagnetic sound methods]. 22 29

The dependence from temperature and viscosity of the shifts of the internal and external wide extremums in the ESR spectra of spin labelled bovine serum albumin has been studied. 2,2,6,6-tetramethylpiperidine-NI-oxyl-4-iodacetamide was used as a spin label. The obtained dependences was shown to be a consequence of the label participation in two types of rotations: an anisotropic fast rotation with tau less than 10(-9) sec relatively to a macromolecule, and the isotropic one with tau greater than 10(-8) sec due to rotation of the macromolecule itself. These conclusions were done on the basis of a model for complex rotation of the spin label. Comparison of theoretical and experimental data makes it possible to determined the correlation time for the protein moiety, to evaluate quantitatively the polarity of surroundings of the iminoxyl and to introduce a numerical parameter for the degree of mobility of the spin label relatively to protein molecule.
Mol Biol (Mosk)
PMID:[Macromolecule rotative correlation time measurement by ESR for covalently bound spin label]. 22 33


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