scholarly journals The Activity of Native Vacuolar Proton-ATPase in an Oscillating Electric Field – Demystifying an Apparent Effect of Music on a Biomolecule

2021 ◽  
Vol 8 ◽  
Author(s):  
Pál Petrovszki ◽  
Krisztina Sebők-Nagy ◽  
Tibor Páli
Keyword(s):  
Electric Field ◽  
Specific Activity ◽  
Membrane Vesicles ◽  
Apparent Effect ◽  
High Concentration ◽  
Membrane Charge ◽  
Proton Atpase ◽  
Rational Explanation ◽  
Oscillating Electric Field ◽  
Fourier Spectra

The effect of an oscillating electric field generated from music on yeast vacuolar proton-ATPase (V-ATPase) activity in its native environment is reported. An oscillating electric field is generated by electrodes that are immersed into a dispersion of yeast vacuolar membrane vesicles natively hosting a high concentration of active V-ATPase. The substantial difference in the ATP hydrolysing activity of V-ATPase under the most stimulating and inhibiting music is unprecedented. Since the topic, i.e., an effect of music on biomolecules, is very attractive for non-scientific, esoteric mystification, we provide a rational explanation for the observed new phenomenon. Good correlation is found between changes in the specific activity of the enzyme and the combined intensity of certain frequency bands of the Fourier spectra of the music clips. Most prominent identified frequencies are harmonically related to each other and to the estimated rotation rate of the enzyme. These results lead to the conclusion that the oscillating electric field interferes with periodic trans-membrane charge motions in the working enzyme.

Parametric excitation in an inhomogeneous plasma

1971 ◽  
Vol 5 (1) ◽  
pp. 107-113 ◽  
Author(s):  
C. S. Chen
Keyword(s):  
Electric Field ◽  
Parametric Excitation ◽  
Growth Rates ◽  
Inhomogeneous Plasma ◽  
Electron Plasma ◽  
Transverse Waves ◽  
Circularly Polarized ◽  
Polarized Waves ◽  
Oscillating Electric Field ◽  
Unmagnetized Plasma

An infinite, inhomogeneous electron plasma driven by a spatially uniform oscillating electric field is investigated. The multi-time perturbation method is used to analyze possible parametric excitations of transverse waves and to evaluate their growth rates. It is shown that there exist subharmonic excitations of: (1) a pair of transverse waves in an unmagnetized plasma and (2) a pair of one right and one left circularly polarized wave in a magnetoplasma. Additionally, parametric excitation of two right or two left circularly polarized waves with different frequencies can exist in a magnetoplasma. The subharmonic excitations are impossible whenever the density gradient and the applied electric field are perpendicular. However, parametric excitation is possible with all configurations.

Oscillating Electric Field Effects on Adsorption of the Methane–Water System on Kaolinite Surface

2018 ◽  
Vol 32 (11) ◽  
pp. 11440-11451 ◽  
Author(s):  
Yudou Wang ◽  
Bo Liao ◽  
Zhaoyang Kong ◽  
Zhigang Sun ◽  
Li Qiu ◽  
...  
Keyword(s):  
Electric Field ◽  
Water System ◽  
Electric Field Effects ◽  
Field Effects ◽  
Oscillating Electric Field ◽  
Kaolinite Surface

scholarly journals Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004 ◽  
Vol 384 (3) ◽  
pp. 507-513 ◽  
Author(s):  
Salvador HERRERO ◽  
Joel GONZÁLEZ-CABRERA ◽  
Juan FERRÉ ◽  
Petra L. BAKKER ◽  
Ruud A. de MAAGD
Keyword(s):  
Bacillus Thuringiensis ◽  
Spodoptera Exigua ◽  
Brush Border Membrane ◽  
Specific Activity ◽  
Membrane Vesicles ◽  
Wild Type ◽  
Oligomeric Form ◽  
Specific Receptors ◽  
Domain Iii

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541–544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S. exigua were determined for all toxins. Compared with Cry1Ca, the affinity of mutant pPB19 was slightly affected (2-fold lower), whereas the affinity of the mutants with an altered domain III (pPB20 and pPB21) was approx. 8-fold lower. Activation of Cry1Ca protoxin by incubation with S. exigua or M. sexta BBMV revealed the transient formation of an oligomeric form of Cry1Ca. The presence of this oligomeric form was tested in the activation of the different Cry1Ca mutants, and we found that those mutated in domain II (pPB19 and pPB21) could not generate the oligomeric form when activated by S. exigua BBMV. In contrast, when oligomerization was tested using BBMV prepared from M. sexta, all of the Cry1Ca mutants showed the formation of a similar oligomeric form as did the wild-type toxin. Our results show how modification of insect specificity can be achieved by manipulation of different parts of the toxin structure involved in different steps of the mode of action of B. thuringiensis toxins.

scholarly journals Molecular and Insecticidal Characterization of a Cry1I Protein Toxic to Insects of the Families Noctuidae, Tortricidae, Plutellidae, and Chrysomelidae

2006 ◽  
Vol 72 (7) ◽  
pp. 4796-4804 ◽  
Author(s):  
Iñigo Ruiz de Escudero ◽  
Anna Estela ◽  
Manuel Porcar ◽  
Clara Martínez ◽  
José A. Oguiza ◽  
...  
Keyword(s):  
Specific Activity ◽  
Membrane Vesicles ◽  
Lobesia Botrana ◽  
Water Soluble ◽  
Insect Species ◽  
Pcr Analysis ◽  
Cry Protein ◽  
Toxic Activity ◽  
Reading Frame

ABSTRACT The most notable characteristic of Bacillus thuringiensis is its ability to produce insecticidal proteins. More than 300 different proteins have been described with specific activity against insect species. We report the molecular and insecticidal characterization of a novel cry gene encoding a protein of the Cry1I group with toxic activity towards insects of the families Noctuidae, Tortricidae, Plutellidae, and Chrysomelidae. PCR analysis detected a DNA sequence with an open reading frame of 2.2 kb which encodes a protein with a molecular mass of 80.9 kDa. Trypsin digestion of this protein resulted in a fragment of ca. 60 kDa, typical of activated Cry1 proteins. The deduced sequence of the protein has homologies of 96.1% with Cry1Ia1, 92.8% with Cry1Ib1, and 89.6% with Cry1Ic1. According to the Cry protein classification criteria, this protein was named Cry1Ia7. The expression of the gene in Escherichia coli resulted in a protein that was water soluble and toxic to several insect species. The 50% lethal concentrations for larvae of Earias insulana, Lobesia botrana, Plutella xylostella, and Leptinotarsa decemlineata were 21.1, 8.6, 12.3, and 10.0 μg/ml, respectively. Binding assays with biotinylated toxins to E. insulana and L. botrana midgut membrane vesicles revealed that Cry1Ia7 does not share binding sites with Cry1Ab or Cry1Ac proteins, which are commonly present in B. thuringiensis-treated crops and commercial B. thuringiensis-based bioinsecticides. We discuss the potential of Cry1Ia7 as an active ingredient which can be used in combination with Cry1Ab or Cry1Ac in pest control and the management of resistance to B. thuringiensis toxins.

scholarly journals SELECTIVE RELEASE OF CONTENT FROM MICROSOMAL VESICLES WITHOUT MEMBRANE DISASSEMBLY

1974 ◽  
Vol 61 (3) ◽  
pp. 789-807 ◽  
Author(s):  
Gert Kreibich ◽  
David D. Sabatini
Keyword(s):  
Serum Proteins ◽  
Specific Activity ◽  
Membrane Vesicles ◽  
Rat Serum ◽  
Coomassie Blue ◽  
Specific Subset ◽  
Low Levels ◽  
Almost All

Rough and smooth microsomes were shown to have similar sets of polypeptide chains except for the proteins of ribosomes bound to the rough endoplasmic reticulum (ER). More than 50 species of polypeptides were detected by acrylamide gel electrophoresis, ranging in molecular weight from 10,000 to approximately 200,000 daltons. The content of rough and smooth microsomes was separated from the membrane vesicles using sublytic concentrations of detergents and differential centrifugation. A specific subset of proteins which consisted of approximately 25 polypeptides was characteristic of the microsomal content. Some of these proteins showed high rates of in vivo incorporation of radioactive leucine or glucosamine, but several others incorporated only low levels of radioactivity within short labeling intervals and appeared to be long-term residents of the lumen of the ER. Seven polypeptides in the content subfractions, including serum albumin, contained almost 50% of the leucine radioactivity incorporated during 5 min and cross-reacted with antiserum against rat serum. Almost all microsomal glycoproteins were at least partly released with the microsomal content. Smooth microsomes contained higher levels of albumin than rough microsomes, but after short times of labeling with [3H]leucine the specific activity of albumin in the latter was higher, supporting the notion that newly synthesized serum proteins are transferred from rough to smooth portions of the ER. On the other hand, after labeling for 30 min with [3H]glucosamine, smooth microsomes contained higher levels of radioactivity than rough microsomes. This would be expected if glycosidation of newly synthesized polypeptides proceeds during their transit through ER cisternae. The labeling pattern of membrane proteins in microsomes obtained from animals which received three daily injections of [3H]leucine, the last administered 1 day before sacrifice, followed the intensity of bands stained with Coomassie blue, with a main radioactive peak corresponding to cytochrome P 450. After the long-term labeling procedure most content proteins had low levels of radioactivity; this was especially true of serum proteins which were highly labeled after 30 min.

Adaptation of phosphate transport in phosphate-deprived LLC-PK1 cells

1985 ◽  
Vol 248 (1) ◽  
pp. F122-F127 ◽  
Author(s):  
J. Caverzasio ◽  
C. D. Brown ◽  
J. Biber ◽  
J. P. Bonjour ◽  
H. Murer
Keyword(s):  
Adaptive Response ◽  
Apical Membrane ◽  
Specific Activity ◽  
Membrane Vesicles ◽  
Phosphate Transport ◽  
Linear Process ◽  
Transport Systems ◽  
Experimental Systems ◽  
Cotransport System ◽  
Dependent Transport

Sodium-dependent transport of phosphate was studied in LLC-PK1 cells that had been deprived of phosphate (Pi). Compared with control cells (fed with 2 mM Pi) a twofold increase in the rate of Na-Pi cotransport was observed in cells incubated for 15 h in a phosphate-free medium, whereas transport of L-alanine and the specific activity of alkaline phosphatase were not changed. The same adaptive response was observed with apical membrane vesicles isolated from Pi-deprived cells. In both experimental systems Pi deprivation caused a change in the Vmax but not in the apparent Km (for Pi) of the cotransport system. Adaptation of the Na-Pi cotransport was triggered by free phosphate concentrations between 0 and 100 microM. Over the first 20 h the adaptive response was found to be a linear process that could be prevented by 70 microM cycloheximide. Adapted cells that were re-treated with phosphate showed a rapid (less than 3 h) decrease in the Na-Pi transport. The data suggest that LLC-PK1 cells adapt to low Pi conditions by increasing the rate of the Na-Pi cotransport, which is located in the apical membrane. Two mechanisms may be involved in the adaptive response: a long-term process involving new protein synthesis, and a short-term response involving activation-inactivation of transport systems already existing.

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