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At least 127 records · Page 7Linked to original sources
PubMed1977

[Microbial growth on an expansion joint of a reservoir for drinkingwater (author's transl)].

In a clear water reservoir built in ready construction after a working-period of five months quite a lot of slime could be found on the expansion joint filled with tightening compound on the base of Thiokol. The covering slime could be removed easily with a rubber-screen. The microbiological analysis showed an extremely high number of colonies and additional the slime was secondarily settled with Protozoa. An influence on the water in the reservoir could not be found out under working conditions.

Chlorides↗
PubMedDate not supplied

[Kinetic characteristics of DNA alkylation with some chloroethylmethylarylamines and elimination of alkylated bases from DNA].

Kinetics of DNA alkylation with 2',3'-o-[N-2-chloroethyl-N-methylamino)benzylidene]uridine (UCHRCL), uridine-5'-methylphosphate (MepUCHRCL) and 4-(N-2-chloroethyl-N-methylamino)benzylamine (NH2CH2RCl) and kinetics of elimination of alkylated bases have been studied. Efficiency of DNA alkylation (p/s-ratio of rate constant of alkylation to the sum of rate constants of by-reactions of an active intermediate formed from the reagent) increases with an increase of the positive charge of the reagents as well as efficiency of tRNA alkylation. Alkylated bases are eliminated from DNA; rate of elimination depends on the structure of the reagent; it decreases in the series NH2CH2R- greater than greater than UCHR-greater than MepUCHR-. Bases alkylated by NH2CH2RCl and UCHRCl are eliminated from DNA during alkylation; therefore plots of DNA alkylation by NH2CH2RCl have a maximum. DNA alkylated by MepUCHRCl is rather stable; alkylated bases are not eliminated during alkylation. Effect of temperature and pH on elimination has been studied.

Alkylating Agents↗
PubMedDate not supplied

[Isolation and properties of polyphosphatase of Neurospora crassa].

Polyphosphatase (polyphosphate-phosphohydrolase) has been isolated from mycelium of Neurospora crassa and purified to homogenous state. The enzyme is shown to be strictly specific to high molecular weight inorganic polyphosphates. Km for phosphate in polymeric form is 6.8-10(-4) M. The molecular weight of this enzyme is 50 000 +/- 3000. To display its activity polyphosphatase requires the presence of bivalent cations of some metals, Mg2+ ions being the best activator with Co2+, Mn2+ and Fe2+ ions-slightly less effective.

Cations, Divalent↗
PubMedDate not supplied

[Isolation of rat liver chromatin non-histone protein].

A chromatin with the protein/DNA ratio of 3.0 was obtained from rat liver cells nuclei. The chromatin was dissolved in 2 M NaCl, pH 7, and reprecipitated by decreasing the ionic strength to 0.4 and increasing pH to 9.0. A fraction of non-histone proteins (NH-1) remained in a supernatant solution, the NH-1/DNA ratio being equal to 1.3 and the ratio of acidic to basic aminoacid residues equal to 1.31. After chromatography on Bio-Rex 70 cation-exchang resin, a fraction (NH-2) with the NH-2/DNA ratio of 1.0 +/- 0.15 and the ratio of acidic to basic aminoacid residues of 1.57 was obtained. According to the data of polyacrylamide gel electrophoresis, the NH-2 fraction contained 2.7% of histone f2 + f3 as an admixture whereas histone f1 was not revealed.

Amino Acids↗
PubMedDate not supplied

[pH-dependence of the mechanism of pepsin action].

N-Acetyl-L-phenylalanine inhibition of the peptic hydrolysis of N-acetyl-L-phenylalanine-L-tyrosine over the pH range 2-4.5 was studied. The mixed character of inhibition which was partially competitive and partially non-competitive allowed us to infer that the separate steps of the enzymatic hydrolysis were pH dependent. The orderliness of the dissociation of the triple enzyme-product-product complex was also pH dependent. The group with pKa approximately 3 influenced the mechanisms of pepsin hydrolysis as strongly as in the case of pepsin catalyzed oxygen isotopic exchange in the acyl amino acid carboxyl group.

Binding Sites↗
PubMed1975

Effect of variations in pH on kinetics of myosin.

The pH optimum was the same in canine tissue for cardiac and skeletal muscle myosin; when myosin was activated by monovalent cations, the pH optimum was 7.5 while activation of myosin by divalent cations gave a pH optimum of 5.5. Protons were needed for divalent cation activation of myosin. With changes in pH there were concomitant changes in the apparent affinity of enzyme for substrate (S 0.5), such that with a decrease in pH there was an elevation in K+- or NH4+ -activated myosin's apparent affinity for adenosine triphosphate (ATP), and at the same time a decrease in Vmax values of myosin. The converse was true with the divalent cations, Ca++ and Mn++; here with a decrease in pH there was a concomitant decrease in apparent affinity of myosin for ATP, and at the same time an increase in the enzymatic Vmax values. It appeared that hydrogen ions affected the apparent affinity of myosin for substrate and this in turn affected the rate-limiting step in ATPase reaction. Addition of monovalent cations to the divalent cation activating system lowered the activity of myosin, and the converse was true: divalent cations lowered the activity of myosin when activated by monovalent ones in a monovalent cation activating system.

Adenosine Triphosphatases↗
PubMed1975

Normal blood-gas values in lambs during neonatal development and in adult sheep.

Arterial oxygen (PaO2) and carbon dioxide (PaCO2) tensions and pH were determined in 20 lambs during development from two weeks to five months of age and in 34 adult sheep. Throughout the period the lambs' mean PaCO2 (33.1 mm Hg) and pH (7.46) values were similar to those determined in the adult sheep (PaCO232.1 mm Hg; pH 7.48). The lamb's mean PaO2 increased from 63.3 mm Hg at two weeks of age to about 80 mm Hg at eight weeks and by 20 weeks was similar to the mean PaO2 (88.0 mm Hg) of adult sheep.

Animals↗
PubMed1975

Identification of dimethylnitrosoamine metabolites in vitro.

The incubation of dimethylnitrosoamine (DMNA) in the presence of rat liver microsomes leads to production of formaldehyde, formic acid, methylamine, and N-methylhydrazine. When pH 5-enzymes are added to the medium there is also the formation of N-methylhydroxylamide and N,N-dimethylhydrazine. The last compound is the only metabolite produced, to a lesser extent, by the pH 5-enzymes. Thus, the denitrosated or non-denitrosated metabolites are produced either by an oxidative dealkylation and by a reduction of DMNA, catalysed by microsomal and cellular soluble enzymes.

Animals↗
PubMed1975

Degradation of dimethylnitrosoamine catalysed by physical and chemical agents.

Decomposition of dimethylnitrosoamine (DMNA) by chemical and physical agents was further investigated. Both photoirradiation with sunlight or ultraviolet ray and reductive reactions under acid conditions (likely occurring in the stomach) led to the formation of formaldehyde, formic acid, and N-methydrazine, in addition to denitrosated compounds such as methylamine, dimethylamine, and N-methylhydroxylamine. N-Methylhydrazine was the only compound which was not detected by photoirradiation under neutral conditions. The agreement between physiochemical and metabolic degradation products and the possible biological meaning are discussed together with the problem of environmental contamination by the nitroso compound.

Dimethylnitrosamine↗
PubMed1976

Hydrogen exchange at the amide group of reduced pyridine nucleotides and the inhibition of that reaction by dehydrogenases.

Stopped flow ultraviolet spectroscopy has been used to measure the rate of hydrogen exchange with solvent at the amide group of reduced nicotinamide nucleotide coenzymes. Several mechanisms for the exchange reaction are considered in the light of the kinetic data. Complex formation between the coenzyme and any of four dehydrogenases markedly slows the rate of hydrogen exchange. Hydrogen bond formation and/or hydrophobic interactions within these complexes are thought to be the reasons for the decreased rate of exchange.

Alcohol Oxidoreductases↗
PubMedDate not supplied

[A compact form of DNA in solution. 2. Peculiarities of acidic titration of double-stranded DNA in PEG-containing water-salt solutions].

The formation of compact double-stranded DNA molecules in PEG-containing watersalt solutions (0.3 M NaCl) may be observed within the pH-range 3-10; i.e. under conditions at which parameters of double-stranded DNA helices are not strongly different from those of B-form. At pH less than 3, when regularity of double helices is significantly changed, the formation of the specific compact particles of DNA in PEG-containing solutions does not take place. Denaturation of the compact form of DNA in PEG-containing solution is accompanied by disappearance of the negative band in CD spectrum. Hyperchromic effect of denaturation of DNA compact form is uninformative because of the influence of the light-scattering by compact DNA molecules.

Circular Dichroism↗
PubMedDate not supplied

[Metabolic acidosis and intravenous injections of fat emulsions (role of phospholipids. Experimental study)].

In explanation of metabolic acidosis during parenteral nutrition, the authors considered the supply of H+ ions by fat emulsion, containing phospholipids of egg or soy. During intravenous infusions of 24 grams of lecithins to two healthy subjects, they observed an increased output H+ ions in urine, about 74,05 and 75,88 mEq, and a metabolic acidosis of the plasma. The theorically forcasted supply of production was 74,6 mEq. Indeed the metabolism of phospholipids supplies phosphoric ions (PO4H3), giving H+ ions at pH 7,40. The most used fat emulsions are able to give between 37 (intralipid 10%) and 61 (lipihysan 15%) mEq of H+ ions/liter.

Acidosis↗