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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of sampling conditions on the levels of adenine nucleotides, pyridine nucleotides, glycolytic intermediates and related metabolites in yeast has been studied. A systematic examination of the conditions for harvesting has shown that it can be best accomplished by rapid filtration. Delays in the handling for removal of the medium, as is usual in the process of obtaining a number of data reported in the literature, lead to important changes in some of the metabolites examined. It is also shown that when a washing is imperative it can be carried out with a methanol-water mixture (50/50, v/v) cooled at -40 degrees without loss of intracellular concentrations of non-readily diffusible metabolites. On the basis of this experience the outline of a generally applicable procedure is presented.
Mol Cell Biochem 1976 Nov 30
PMID:Determination of intermediary metabolites in yeast. Critical examination of the effect of sampling conditions and recommendations for obtaining true levels. 1 64

The temperature dependencies of the photoconversion of pigments P870--P890 were studied using isolated chromatophores and photosynthetic reaction centres (RC's) of purple bacteria. The samples were prepared by extraction with organic solvents (light petroleum and a combination of light petroleum and methanol) and modified through cross-linking the functional groups of proteins by treatment with glutaraldehyde or denatured by various physical and chemical treatments. The data provide further evidence that the pool of RC secondary acceptors is formed by the compounds of quinone nature located in the hydrophobic surrounding. Similar molecules localized in a more polar medium act as primary acceptors. The findings indicate on the essential role of macromolecular components in the RC's functioning and also suggest that the photochemical charge separation is conformation-controlled.
Mol Biol (Mosk)
PMID:[Possible role of macromolecular components in the functioning of photosynthetic reaction centers of purple bacteria]. 10 47

Yeast cells (Saccharomyces cerevisiae) were grown in the presence of [14C]phenylalanine and pulse-labelled with [3H]phenylalanine in the presence of cycloheximide. The proteins extractable into chroloform: methanol (2:1) were isolated from mitochondria and analysed by SDS gel filtration. Four protein fractions varying in molecular weight were separated. In order to identify the transcriptional origin and the site of protein synthesis ethidium bromide was used. Different sensitivity of protein syntheses to various concentrations of ethidium was shown. These data are discussed in relation to the possible presence of two classes of membrane-bound polyribosomes in mitochondria.
Mol Cell Biochem 1977 Feb 04
PMID:Intramitochondrial synthesis of membrane proteins in yeast: differential inhibition by ethidium. 32 93

Earlier we have shown that DNA forms stoichiometric complexes with bis-(2-guanidoethyl)-disulfide (GED), the helix being transformed from the B-like structure into the C-like one. The present work demonstrates that the DNA helix in the saturated complex does not change its conformation within a broad range of conditions: 0 less than [NaCl] less than 5.10(-2) M; 0% less than [methanol] less than 60% (v/v); 5 degrees less than temperature less than 50 degrees. Free DNA undergoes a non-cooperative winding within the B-family under all these influences. Increase in NaCl concentration beyond 5.10(-2) M results in abrupt cooperative unwinding from the C-like form to the B-like one, apparently due to GED dissociation. The obtained data are in accord with the idea that the conformational transition of DNA within the B-family is induced by change of phosphates interaction with the hydrated cations of alcaline metals; formation of strong hydrogen bonds of the phosphates with GED makes the DNA helix non-sensitive to variations of the environment.
Mol Biol (Mosk)
PMID:[Bis-(2-guanidoethyl)-disulfide, when complexed with DNA, prevents its winding within the B-family]. 46 Jan 89

Kinetic of the alpha-chymotrypsin catalyzed reversible hydrolytic reaction of methyl N-acetyl-L-phenylalaninate and N-acetyl-L-phenylalanylglycinamide at pH 5.5 and equilibrium conditions has been studied. The rates of the labeled reaction products incorporated into the substrate a different methanol concentrations shows that the reaction proceeds by a compulsory mechanism with the formation of N-acetyl-L-phenylalanine-alpha-chymotrypsin complex. For the amide substrate the data obtained are also in agreement with the compulsory mechanism of its hydrolysis. Equilibrium kinetics of ester and amide substrates hydrolysis has been compared.
Mol Biol (Mosk)
PMID:[Kinetics of alpha-chymotrypsin catalyzed hydrolysis in equilibrium. II. Comparison of ester and amide substrates]. 61 42

Some properties of a submitochondrial cell-free system for protein synthesis are described. The system was prepared from rat liver mitochondria lysed with Triton X-100, and the lysate was characterized by a linear rate of [14C]amino acid incorporation for 15-20 min with subsequent decline in activity. The incorporation reaction was inhibited by chloramphenicol and was insensitive to cycloheximide. Poly(U) addition stimulated [14CA1phenylalanine incorporation by the preincubated submitochondrial system. Upon the addition of 7.5S mRNA that was isolated from mitochondria the major translation product was identified as a hydrophobic poly-peptide which in some properties (solubility in chloroform-methanol mixture) was similar to one of polypeptides synthesized by the sub-mitochondrial system on endogeneous mRNAs.
Mol Cell Biochem 1977 Feb 04
PMID:On the cell-free system of protein synthesis from mammalian mitochondria. 85 30

Infrared spectra (in the region of 1800-1600 cm-1) of aggregated protochlorophyll, chlorophyll a and b, bacterioviridin, protopheophytin, pheophytin a (in the solid films) with different absorption spectra were studied. The formation of various types of aggregates is due to the realization of different modes of intermolecular bonding. The mode of interaction depends upon the chemical structure of the pigment and upon the inclusion of low-molecular addenda into the structure of aggregates. The forms 677 nm of chlorophyll a and 658 nm of chlorophyll b appear when the coordination bonds between the keto groups of the cyclopentanone ring and central magnesium atom are formed. The longwave forms of chlorophyll a (745 nm) and chlorophyll b (675 nm, 725 nm) are formed when methanol molecules are involved in the intermolecular bonds. The coordination bonds between C=O and magnesium atom in the longwave aggregate of bacterioviridin (750 nm) are observed without participation of the low-molecular addenda, The formation of the protochlorophyl 635 nm form and aggregated forms of magnesium-free pigments occurs without participation of carbonyl groups probably by direct interaction between the eta-electron systems of molecules. The frequencies of carbonyl groups of the solid films in dioxane vapours causing absorption maxima at 690 nm (chlorophyll a) and 670 nm (chlorophyll b) are not shifted as compared to the dissolved pigments. Thipoints to the intermolecular interaction without participation of C=O groups.
Mol Biol (Mosk)
PMID:[Molecular organization of aggregated forms of chlorophyll and its analogs]. 95 22

By computer calculation with the use of atom-atom potentials a stereochemical model of the DNA-hydrate Na+ complex was obtained according to which the Na+(H2O)6 octahedrons are localized in the narrow groove of DNA with formation of a great number of van der vaals contacts and hydrogen bonds. The model explains why the C-form of DNA is stabilized in the Na-DNA complex which is formed in the presence of 80% methanol (v/v). A possibility of the existence of such complexes in vivo at the DNA regions surrounded with media of diminished water activity (the DNA-membrane complex, chromosomes, phage heads) is discussed.
Mol Biol (Mosk)
PMID:[A stereochemical model for DNA-Na+ (H20) complex]. 121 76

The incorporation of 32P into well washed human erythrocyte membranes was studied in a medium containing [gamma-32P]ATP, Mg2+, and EGTA. Following phosphorylation, the membranes were completely solubilized in 1% sodium dodecyl sulfate and subjected to gel electrophoresis in dodecyl sulfate polyacrylamide. A large incorporation of radioactivity was observed in a band which migrated faster than component 7 (nomenclature of T. L. Steck, (1972), J. Mol. Biol. 66, 295) but slower than the bromophenol blue tracking dye, and did not stain with Coomassie Blue. Isolation of this band by preparative gel electrophoresis revealed that 41% of the radioactivity was associated with a 32P-labeled polypeptide. This polypeptide was further purified by gel chromatography on Sephadex LH-20 in chloroform-methanol-HCl, and Bio-Gel A 1.5m in dodecyl sulfate. Its amino acid composition is characterized by a high content of acidic residues. The calculated minimal molecular weight is 15084. Based upon the recovery of amino acids, the polypeptide fraction comprises at least 1.8% by weight of the total erythrocyte membrane proteins. An apparent molecular weight of 15000 was estimated by gel chromatography in dodecyl sulfate, while a range of 14000-16000 was estimated by electrophoresis in dodecyl sulfate polyacrylamide. The state of phosphorylation of this peptide may reflect a physiological function in the intact red cell.
 ...
PMID:Isolation of a 32P-labeled polypeptide of low molecular weight from phosphorylated human erythrocyte membranes. 124 9

(S)-1-[3-Hydroxy-2-(phosphonylmethoxy)propyl]cytosine (HPMPC) is an antiviral phosphonate nucleotide analogue that displays activity against a range of herpesviruses. Anion exchange high performance liquid chromatography analysis of the 60% methanol extract from [14C]HPMPC-treated cells reveals the formation of three major metabolites. Two of these were identified as phosphorylated forms of HPMPC, HPMPC phosphate, and HPMPC diphosphate, by liberation of HPMPC upon acid digestion and coelution with synthetic standards on high performance liquid chromatography. The third metabolite, which is resistant to alkaline phosphatase cleavage but sensitive to phosphodiesterase, is proposed to be an HPMPC phosphate adduct. In herpes simplex virus-1-infected cells the same three metabolites are detected, at concentrations comparable to those in uninfected cells. When HPMPC is removed from the medium, the concentrations of the metabolites in cells decrease slowly, with half-lives of approximately 6, 17, and 48 hr for HPMPC phosphate, HPMPC diphosphate, and the HPMPC phosphate adduct, respectively. HPMPC diphosphate inhibits herpes simplex virus-1 and -2 DNA polymerases with a lower Ki than that for DNA polymerase alpha, and enzyme inhibition is competitive in each case. The formation and the persistence of HPMPC phosphates in cells and the selective inhibition of viral DNA polymerases by HPMPC diphosphate can explain why cells pretreated with HPMPC remain refractory to viral infection even long after HPMPC is removed from the medium.
Mol Pharmacol 1992 Jan
PMID:Intracellular metabolism of the antiherpes agent (S)-1-[3-hydroxy-2-(phosphonylmethoxy)propyl]cytosine. 131 Jan 43


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