Permeabilized-Cell Internal Solution (350 µm EGTA):

2015 ◽  
Vol 2015 (5) ◽  
pp. pdb.rec079657
Keyword(s):  
Permeabilized Cell ◽  
Internal Solution

scholarly journals Indirect Drying and Coking Characteristics of Coking Coal with Soda Residue Additive

Energies ◽  
2021 ◽  
Vol 14 (3) ◽  
pp. 575
Author(s):  
Ze Zhang ◽  
Shuting Zhang
Keyword(s):  
Energy Saving ◽  
Drying Characteristics ◽  
Coking Coal ◽  
Internal Solution ◽  
Active Point ◽  
System A ◽  
Dry Distillation ◽  
Drying Rates ◽  
Process Energy ◽  
Drying Efficiency

To improve indirect drying efficiency, the effect of soda residue on the drying characteristics of coking coal were studied using a self-made indirect drying system. A tube furnace was used in the dry distillation of coal samples with soda residue, and the coke properties were analyzed. The results indicated that the soda residue has a significant influence on the increase in the heating rate of coal samples in the temperature distribution range of 90 to 110 °C. With the addition of 2%, 5%, and 10% soda residue, the drying rates increased by 11.5%, 25.3%, and 37.3%, respectively at 110 °C. The results of dry distillation show that addition of 2%, 5% and 10% soda residue decreases the carbon loss quantity by 4.67, 4.99, and 8.82 g, respectively. The mechanical strength of coke samples satisfies the industrial conditions when the soda residue ratio ranges from 2% to 5%. Soda residue can improve the active point of coke dissolution reaction and inhibit coke internal solution. Economically, coking coal samples mixed with soda residue have an obvious energy saving advantage in the drying process. Energy saving analysis found that it can reduce cost input by 20% than that of the normal drying method.

scholarly journals Membrane capacitance in frog cut twitch fibers mounted in a double vaseline-gap chamber.

1990 ◽  
Vol 96 (2) ◽  
pp. 225-256 ◽  
Author(s):  
W K Chandler ◽  
C S Hui
Keyword(s):  
Plasma Membranes ◽  
Unit Length ◽  
Electrical Measurements ◽  
Tetraethylammonium Chloride ◽  
Internal Solution ◽  
Current Passing ◽  
Longitudinal Resistance ◽  
Small Change ◽  
Internal Longitudinal Resistance ◽  
Earth Potential

In experiments on cut muscle fibers mounted in a double Vaseline-gap chamber, electrical measurements are usually made by measuring the voltage V1(t) in one end pool and by passing current I2(t) from the other end pool to the central pool, which is usually clamped to earth potential. The voltage in the current-passing end pool is denoted by V2(t). This article describes how the value of the holding current, Ih, and the values of delta V2(infinity)/delta V1(infinity) and delta I2(infinity)/delta V1(infinity) that are associated with a small change in V1(t) can be used to estimate the linear cable parameters rm, ri, and re in a cut fiber that has been equilibrated with a Cs-containing internal solution. rm, ri, and re represent, respectively, the resistance of the plasma membranes, the internal longitudinal resistance, and the external longitudinal resistance under the Vaseline seals, all for a unit length of fiber. The apparent capacitance, Capp, of the preparation is defined to equal integral of infinity 0 delta I2,tr(t) dt/delta V1(infinity), in which delta I2,tr(t) represents the transient component of current that is associated with a change in V1(t) of amplitude delta V1(infinity). A method is described to estimate cm, the capacitance of the plasma membranes per unit length of fiber, from Capp and the values of rm, ri, and re. In experiments carried out with a tetraethylammonium chloride (TEA.Cl) solution at 13-14 degrees C in the central pool, cm remained stable for as long as 3-4 h. The values of cm, 0.19 microF/cm on average, and their variation with fiber diameter are similar to published results from intact fibers. This article also describes the different pathways that are taken by the current that flows from the current-passing end pool to the central pool. Approximately two-thirds of delta I2,tr(t) flows across the capacitance of the plasma membranes in the central-pool region. The rest flows either across plasma membranes that are under the two Vaseline seals or directly from the current-passing end pool to the central pool, across the external longitudinal resistance under the Vaseline seal. [There is also a current that flows directly from the voltage-measuring end pool to the central pool but this does not contribute to delta I2,tr(t).]

Pharmaceutical Therapies for Sealing of Permeabilized Cell Membranes in Electrical Injuriesa

1999 ◽  
Vol 888 (1 OCCUPATIONAL) ◽  
pp. 266-273 ◽  
Author(s):  
RAPHAEL C. LEE ◽  
JURGEN HANNIG ◽  
KENNETH L. MATTHEWS ◽  
ADAM MYEROV ◽  
CHIN-TU CHEN
Keyword(s):  
Cell Membranes ◽  
Permeabilized Cell

Role of protein kinase C in T-cell antigen receptor regulation of p21ras: evidence that two p21ras regulatory pathways coexist in T cells

1992 ◽  
Vol 12 (7) ◽  
pp. 3305-3312
Author(s):  
M Izquierdo ◽  
J Downward ◽  
J D Graves ◽  
D A Cantrell
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase Inhibitor ◽  
Antigen Receptor ◽  
Permeabilized Cell ◽  
Regulatory Pathways ◽  
Kinase C ◽  
Stimulation Of

T-lymphocyte activation via the antigen receptor complex (TCR) results in accumulation of p21ras in the active GTP-bound state. Stimulation of protein kinase C (PKC) can also activate p21ras, and it has been proposed that the TCR effect on p21ras occurs as a consequence of TCR regulation of PKC. To test the role of PKC in TCR regulation of p21ras, a permeabilized cell system was used to examine TCR regulation of p21ras under conditions in which TCR activation of PKC was blocked, first by using a PKC pseudosubstrate peptide inhibitor and second by using ionic conditions that prevent phosphatidyl inositol hydrolysis and hence diacylglycerol production and PKC stimulation. The data show that TCR-induced p21ras activation is not mediated exclusively by PKC. Thus, in the absence of PKC stimulation, the TCR was still able to induce accumulation of p21ras-GTP complexes, and this stimulation correlated with an inactivation of p21ras GTPase-activating proteins. The protein tyrosine kinase inhibitor herbimycin could prevent the non-PKC-mediated, TCR-induced stimulation of p21ras. These data indicate that two mechanisms for p21ras regulation coexist in T cells: one PKC mediated and one not. The TCR can apparently couple to p21ras via a non-PKC-controlled route that may involve tyrosine kinases.

scholarly journals A permeabilized cell model for studying cell division: a comparison of anaphase chromosome movement and cleavage furrow constriction in lysed PtK1 cells.

1981 ◽  
Vol 88 (3) ◽  
pp. 618-629 ◽  
Author(s):  
W Z Cande ◽  
K McDonald ◽  
R L Meeusen
Keyword(s):  
Cell Model ◽  
Chromosome Movement ◽  
Microtubule Depolymerization ◽  
Mitotic Apparatus ◽  
Permeabilized Cell ◽  
Culture Cells ◽  
Brij 58 ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Chromosome Movements

After lysis in a Brij 58-polyethylene glycol medium, PtK1 cells are permeable to small molecules, such as erythrosin B, and to proteins, such as rhodamine-labeled FAB, myosin subfragment-1, and tubulin. Holes are present in the plasma membrane, and the mitochondria are swollen and distorted, but other membrane-bounded organelles of the lysed cell model are not noticeably altered. After lysis, the mitotic apparatus is functional; chromosomes move poleward and the spindle elongates. Cells lysed while in cytokinesis will continue to divide for several minutes. Addition of crude tubulin extracts, MAP-free tubulin, or taxol to the lysis medium retards anaphase chromosome movements but does not affect cleavage. On the other hand, N-ethylmaleimide-modified myosin subfragment-1, phalloidin, and cytochalasin B inhibit cleavage but have no effect on anaphase chromosome movements under identical lysis conditions. These results suggest that actomyosin plays no functional role in anaphase chromosome movement in mammalian tissue culture cells and that microtubule depolymerization is a rate-limiting step for chromosome-to-pole movements.

scholarly journals A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation.

1991 ◽  
Vol 115 (5) ◽  
pp. 1225-1236 ◽  
Author(s):  
F J Stafford ◽  
J S Bonifacino
Keyword(s):  
Protein Degradation ◽  
Secretory Pathway ◽  
Fibroblast Cell ◽  
Cell System ◽  
Current Evidence ◽  
Permeabilized Cell ◽  
Intact Cells ◽  
Permeabilized Cells ◽  
Streptolysin O ◽  
A Site

Analysis of the fate of a variety of newly synthesized proteins in the secretory pathway has provided evidence for the existence of a novel protein degradation system distinct from that of the lysosome. Although current evidence suggests that proteins degraded by this system are localized to a pre-Golgi compartment before degradation, the site of proteolysis has not been determined. A permeabilized cell system was developed to examine whether degradation by this pathway required transport out of the ER, and to define the biochemical characteristics of this process. Studies were performed on fibroblast cell lines expressing proteins known to be sensitive substrates for this degradative process, such as the chimeric integral membrane proteins, Tac-TCR alpha and Tac-TCR beta. By immunofluorescence microscopy, these proteins were found to be localized to the ER. Treatment with cycloheximide resulted in the progressive disappearance of intracellular staining without change in the ER localization of the chimeric proteins. Cells permeabilized with the pore-forming toxin streptolysin O were able to degrade these newly synthesized proteins. The protein degradation seen in permeabilized cells was representative of that seen in intact cells, as judged by the similar speed of degradation, substrate selectivity, temperature dependence, and involvement of free sulfhydryl groups. Degradation of these proteins in permeabilized cells took place in the absence of transport between the ER and the Golgi system. Moreover, degradation occurred in the absence of added ATP or cytosol, and in the presence of apyrase, GTP gamma S, or EDTA; i.e., under conditions which prevent transport of proteins out of the ER. The efficiency and selectivity of degradation of newly synthesized proteins were also conserved in an isolated ER fraction. These data indicate that the machinery responsible for pre-Golgi degradation of newly synthesized proteins exists within the ER itself, and can operate independent of exogenously added ATP and cytosolic factors.

scholarly journals A New method for ISE construction for methyl orange dyes and using for indirect determination of Amitriptyline Hydrochloried drug

2015 ◽  
Vol 12 (1) ◽  
pp. 188-196
Author(s):  
Baghdad Science Journal
Keyword(s):  
Methyl Orange ◽  
Response Time ◽  
Electrode Surface ◽  
Ion Pair ◽  
New Method ◽  
Ion Selective Electrode ◽  
Selective Electrode ◽  
Internal Solution ◽  
Indirect Determination

A new method for construction ion-selective electrode (ISE) by heating reaction of methyl orange with ammonium reineckate using PVC as plasticizer for determination methyl orange and determination Amitriptyline Hydrochloried drug by formation ion-pair on electrode surface . The characteristics of the electrode and it response as following : internal solution 10-4M , pH (2.5-5) ,temperature (20-30) and response time 2 sec. Calibration response for methyl orange over the concentrationrange 10-3 -10-9 M with R=0.9989 , RSD%=0.1052, D.O.L=0.315X10-9 MEre%=(-0.877- -2.76) , Rec%.=(97.230 -101.711) .

scholarly journals Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform

2002 ◽  
Vol 156 (4) ◽  
pp. 653-664 ◽  
Author(s):  
Frédéric Mallard ◽  
Bor Luen Tang ◽  
Thierry Galli ◽  
Danièle Tenza ◽  
Agnès Saint-Pol ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Molecular Mechanisms ◽  
Retrograde Transport ◽  
Cell System ◽  
Permeabilized Cell ◽  
Secretory Pathways ◽  
Recycling Endosomes ◽  
Sequential Action

The molecular mechanisms underlying early/recycling endosomes-to-TGN transport are still not understood. We identified interactions between the TGN-localized putative t-SNAREs syntaxin 6, syntaxin 16, and Vti1a, and two early/recycling endosomal v-SNAREs, VAMP3/cellubrevin, and VAMP4. Using a novel permeabilized cell system, these proteins were functionally implicated in the post-Golgi retrograde transport step. The function of Rab6a' was also required, whereas its closely related isoform, Rab6a, has previously been implicated in Golgi-to-endoplasmic reticulum transport. Thus, our study shows that membrane exchange between the early endocytic and the biosynthetic/secretory pathways involves specific components of the Rab and SNARE machinery, and suggests that retrograde transport between early/recycling endosomes and the endoplasmic reticulum is critically dependent on the sequential action of two members of the Rab6 subfamily.

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