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PubMed1997

Length-reduction method for man-made mineral fibers for biological experiments.

A simple fiber length-reduction method was developed to obtain a large amount of fiber samples with different length distributions for use in various biological experiments. This press method is only to press a raw fiber sample charged in a stainless cylinder at an adequate pressure, and is effective for man-made mineral fibers (MMMF) such as glass wool, rock wool and wool and refractory fibers (ceramic fibers, mullite fibers) and some brittle natural mineral fibers such as fibrous brucite and wollastonite. The mean fiber-length of man-made mineral fibers became shorter with the increase in the pressure applied without diameter change. We could obtain a length-reduced fiber sample with a suitable length distribution by this method. This press method is therefore a size-selective method able to produce a large amount of pulverized fiber sample depending on the press cylinder size for biological experiments. A very small amount of non-fibrous particles with aspect ratios (length vs. diameter) of under 3 was seen in the pulverized fiber samples. To eliminate such non-fibrous particles as well as too long fibers from the sample, separation by sedimentation in water was somewhat effective.

Aluminum Silicates↗
PubMed1975

Enzymic formation of thiamine pyrophosphate in plants.

Evidence was presented by paper chromatographic analysis on the occurrence of an enzyme capable of catalyzing a pyrophosphate transfer from ATP to thiamine in green leaves of various plants. The exclusive localization of the enzyme activity in the 105,000 X g supernatant (in a soluble form) was demonstrated by differential centrifugation of a cell homogentae in 0.25 M sucrose. The enzyme was purified by column chromatography with DEAE-cellulose and by gel filtration with Sephadex G-150. The partially pruified preparation, while contaminated with detectable activity of acid phosphatase, lost the ability of utilizing thiamine monophosphate as the substrate in place of thiamine. These findings lead to the conclusion that thiamine pyrophosphate is formed in green leaves of plants through a direct pyrophosphorylation of thiamine in the presence of ATP and Mg.

Acid Phosphatase↗
PubMed2001

[Biodegradation of polycyclic aromatic hydrocarbons by a preponderant brevibacterium].

A preponderant brevibacterium was isolated from the sludge contaminated by coke-plantwaste water for a long time. The bacterium was effective on the degradation and transformation of anthracene, phenanthrene and pyrene. The degradation process can be accelerated by ferric ions. 10 hours after aeration, the removing rates of anthracene, phenanthrene and pyrene by the brevibacterium were about 75%, 87% and 62% respectively. 106 hours after aeration, the removing rates of total organic carbon (TOC) caused by anthracene, phenanthrene and pyrene were 50%, 90%, and 50% respectively.

Aerobiosis↗
PubMedDate not supplied

[Phosphorescence of octaethylchlorine, isobacteriooctaethylchlorine and their metal complexes].

The phosphorescence of dihydrooctaethylporphin (octaethylchlorin or OEC), of its complexes with magnesium, zinc, copper and palladium, and of zinc and palladium complexes of isobacteriooctaethylchlorin (5,6,7,8-tetrahydrooctaethylporphin with adjacent hydrogenated pyrrole rings or THOEP-ADJ) has been investigated. The phosphorescence spectra and phosphorescence excitation spectra as well as the ratio of fluorescence and phosphorescence yields and the triplet state lifetume have been measured. It has been shown that the singlet-triplet interval is about 4100 cm-1 for OEC complexes and about 4300 cm-1 for THOEP-ADJ complexes, and depends wealky on the nature of the metal atom forming the complex. The triplet level position of chlorophyll alpha is discussed. It is concluded that the maximum of chlorophyll alpha phosphorescence spectrum must be located at 895 nm.

Copper↗
PubMed1976

Catalytic mechanisms of glutamine synthetase enzymes. Studies with analogs of possible intermediates and transition states.

Glutamine synthetase enzymes isolated from pea seeds and from Escherichia coli are observed to behave differently in experiments designed to probe reaction mechanism. Although both enzymes were found to bind and release substrates in random order mechanisms (Wedler, F.C. (1974) J. Biol. Chem, 247, 5080-5087), isotopic exchanges with partial reaction systems indicative of a gamma-glutamylphosphate intermediate are catalyzed only by the pea seed enzyme. The E. coli system fails to catalyze any exchanges at appreciable rates unless all substrates are present. This negative result implies either an absolute conformational requirement for bound substrates or that the putative complex (E-Glu-P-MgADP) is exceedingly tight. To test the latter, a nonreactive structural analog of gamma-glutamyl-phosphate, namely 3-(phosphonoacetylamido)-L-alanine (PA2LA), has been synthesized. With the E. coli enzyme PA2LA was found to bind no more tightly than L-glutamate and is strictly competitive versus L-glutamate (Ki = 3 mM). Thus, failure to catalyze partial exchange reactions indicative of gamma-Glu-P is probably not attributable to tight complex formation. The binding of PA2LA with the pea seed enzyme apparently involves a two-step process: a rapid, reversible step in which PA2LA binds 10-fold more tightly than L-glutamate, followed by a slow (but reversible) process involving very tight PA2LA binding, apparently with enzyme isomerization promoted by nucleotide. The specificity of the two enzymes toward L-methionine-SR-sulfoximine, Met(O)(NH), was also different...

Adenosine Diphosphate↗
PubMed1976

Interaction of anions and divalent metal ions with phosphoenolpyruvate carboxykinase.

The catalytic activity of phosphoenolpyruvate carboxykinase in rat liver cytosol is stimulated by incubating with Fe2+, Mn2+, Co2+, and Cd2+. When purified, the enzyme no longer responds to Fe2+, Co2+, or Cd2+ but retains a response to Mn2+. Low concentrations of SO4(2-) in the incubation medium with enzyme and divalent transition metal allow stimulation by Fe2+ and Co2+ and enhance the response to Mn2+. Under identical conditions, orthophosphate with Fe2+ is a potent inhibitor of the enzyme (half-maximal inhibition at 50 muM). A thiol is required in the incubation medium for the effects of Fe2+ plus sulfate or orthophosphate to be expressed. The magnitude of these effects depends on the thiol concentration. Dithiothreitol is more effective than GSH and activation by sulfate plus Fe2+ appears to require the reduced form of dithiothreitol. Sulfate ion is not considered to be the physiological Fe2+-activator of P-enolpyruvate carboxykinase in rat liver cytosol, as this function is fulfilled by a newly discovered liver protein. Knowledge concerning the interaction of Fe2+ and sulfate with the enzyme may be useful in examining their interaction between the enzyme, ferrous ion, and this activator protein.

Acetates↗
PubMed2005

Characteristics of NO reduction with non-thermal plasma.

As a new type of NO removal system, NO reduction in N2-NO plasma was applied to solve the difficulties in the traditional methods, such as higher energy-consumption, larger equipment size and high cost, and so on. Using the experimental NO reduction system with single-pair electrode tip discharge structure, the NO reduction characteristics of N2-NO system were revealed to guide the engineering practice; the results of NO reduction with single-pair electrode tip discharge plasma also have the same instructive meaning to the NO reduction with multi-pair electrode tip discharge plasma. The amount of both active N atom and NO removal rate increased with the distance /g increasing between the two electrode tips and then dropped when the distance exceeded a certain value. The NO removal rate increased while the voltage between two electrode tips or the resident time of gas flow increased. The distance is a key geometrical variable factor that can determine the intensity of electric field between two electrode tips and the resident time of gas. In this paper, the effects of the dielectric features on NO reduction using dielectric-barrier discharge plasma system were also studied. The results of NO removal rate with different dielectrics such as Al2O3, CaO, MgO and glass showed that the electric field intensity is different with different dielectric, because it brings different energy to particles in discharge room and thus it causes different NO removal rate.

Aluminum Oxide↗
PubMed1991

Effect of divalent metal ions on collagenase from Clostridium histolyticum.

The collagenase from Clostridium histolyticum (EC 3.4.24.3) degrades type IV collagen with Km 32 nM, indicating a high affinity for this substrate. Ferrous and ferric ions can inhibit Clostridium collagenase. Inhibition by Fe++ was of the mixed, non-competitive type, with Ki 90 microM. The inhibitory effect of Fe++ may be due to Zn++ displacement from the intrinsic functional center of this metalloprotease, since in the presence of excess amounts of Zn++ enzyme activity is retained. This inhibitory effect of Fe++ may be common for all types of collagenases, since this ion can also inhibit type IV collagenase purified from Walker 256 carcinoma, with IC50 80 microM. Cu++ can only partially inhibit Clostridium collagenase, while other divalent metal ions such as Cd++, Co++, Hg++, Mg++, Ni++ or Zn++ are devoid of any inhibitory effect on the enzyme.

Amino Acid Sequence↗
PubMed1989

The potentiation of norepinephrine-induced contraction of rabbit aorta by Mg2+ deletion in a Ca2+-free medium.

Residual responses to norepinephrine (NE) in an Mg2+-, Ca2+-free medium with low EGTA (0.1 mM) for 15 min were potentiated following preincubation of rabbit aortas in Mg2+-free medium for 60 min. Responses to Ca2+ in a Ca2+-free medium with nifedipine and NE were not affected under a similar Mg2+-free condition. Nifedipine, theophylline, dibutyryl cAMP, 8-bromo-cGMP, methylene blue, La3+ or vanadate did not affect the residual response or the potentiation. However, high EGTA (1 mM) inhibited both the residual response and the potentiation. The residual response to NE was not potentiated following incubation in Mg2+-, Ca2+-free medium for 60 min. These results suggest that, in the rabbit aorta, Mg2+ deletion from the medium selectively potentiates the residual response to NE in a Ca2+-free medium without any effect on the response due to Ca2+-influx through receptor-operated channels. This potentiation does not appear to be related to either the levels of cAMP and cGMP or the activity of an Mg2+-dependent, Ca2+-ATPase.

Animals↗
PubMed1987

The effect of [Mg2+] on the Ca2+ dependence of ATPase and tension development of fast skeletal muscle. The role of the Ca2+-specific sites of troponin C.

Conflicting reports have appeared concerning the effect of [Mg2+] on muscle activity. Several groups have found that increasing [Mg2+] produces a right-ward shift of the pCa-tension curve, while others have found no effect of [Mg2+] on myofibrillar ATPase activity. The present study is a careful evaluation of the effect of [Mg2+] on myofibrillar ATPase, skinned fiber tension development, TnCDANZ (troponin C (TnC)-labeled with 5-dimethylaminonaphthalene-1-sulfonyl aziridine) fluorescence, and simultaneous TnCDANZ fluorescence and tension development in the same fiber. A small effect of [Mg2+] on both ATPase and tension development was found with an apparent association constant of about 2 X 10(2) M-1. The Ca2+ dependence of TnCDANZ fluorescence was similarly effected by [Mg2+], either alone or when incorporated into TnC-depleted skinned fibers (K'Mg approximately equal to 2-3 X 10(2) M-1), suggesting that the effect of [Mg2+] on activity is due to an effect of [Mg2+] on Ca2+ binding to the Ca2+-specific sites of TnC. It is not yet clear whether this effect of [Mg2+] is through direct competition at the binding sites or through indirect effects. In either case, the calculated effect of physiological [Mg2+] is so small that the regulatory sites of TnC can still be considered "Ca2+-specific." In addition, a slightly greater effect of [Mg2+] on tension development (K'Mg = 4.62 X 10(2) M-1) was observed only for very low levels of [Mg2+], which might suggest an additional effect of Mg2+ on tension development which is saturated by millimolar Mg2+.

Animals↗
PubMed1979

Specific perturbation by Ca2+ of tyrosyl residue 138 of calmodulin.

Calmodulin that was selectively nitrated at tyrosyl residue 99 or 138 was used as a regional spectral probe of the structural changes associated with Ca2+ or Mg2+ binding to the protein. Perturbations of the spectral properties of the nitrotyrosyl residues correlated well with those of the tyrosyl residues in unmodified calmodulin. The spectral properties of tyrosyl residue 99 were sensitive to ionic strength, but not to Ca2+ binding to the protein. The spectrum of tyrosyl residue 138, in contrast, was markedly affected both by ionic strength and Ca2+ binding. Although Mg2+ caused spectral changes, they were clearly different from those produced by Ca2+ and resembled instead the less specific changes elicited by Na+. Conformational changes associated with Ca2+ but not Mg2+ binding to calmodulin seem to affect selectively the microenvironment around tyrosyl residue 138.

Calcium↗