Albumin-Induced Endocytic Vacuoles in Tetrahymena Pyrijormis

1975 ◽  
Vol 33 ◽  
pp. 694-695
Author(s):  
L. J. Brenner ◽  
D. G. Osborne ◽  
B. L. Schumaker
Keyword(s):  
Electron Microscopy ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Tetrahymena Pyriformis ◽  
Sequence Of Events ◽  
Cytoplasmic Bodies ◽  
Food Vacuoles ◽  
Mouse Ascites ◽  
Normal Human

Exposure of the ciliate, Tetrahymena pyriformis, strain WH6, to normal human or rabbit sera or mouse ascites fluids induces the formation of large cytoplasmic bodies. By electron microscopy these (LB) are observed to be membrane-bounded structures, generally spherical and varying in size (Fig. 1), which do not resemble the food vacuoles of cells grown in proteinaceous broth. The possibility exists that the large bodies represent endocytic vacuoles containing material concentrated from the highly nutritive proteins and lipoproteins of the sera or ascites fluids. Tetrahymena mixed with bovine serum albumin or ovalbumin solutions having about the same protein concentration (7g/100 ml) as serum form endocytic vacuoles which bear little resemblance to the serum-induced LB. The albumin-induced structures (Fig. 2) are irregular in shape, rarely spherical, and have contents which vary in density and consistency. In this paper an attempt is made to formulate the sequence of events which might occur in the formation of the albumin-induced vacuoles.

Serum-Induced Endocytic Vacuole in the Nonphagocytic Tetrahymena Pyriformis Strain NP1

1977 ◽  
Vol 35 ◽  
pp. 644-645
Author(s):  
L. J. Brenner ◽  
D. G. Osborne ◽  
B. L. Schumaker
Keyword(s):  
Electron Microscopy ◽  
Large Body ◽  
Tetrahymena Pyriformis ◽  
Metal Salts ◽  
Proteose Peptone ◽  
Transmission Electron ◽  
Food Vacuoles ◽  
Heavy Metal Salts ◽  
Normal Human ◽  
Peptone Medium

Tetrahymena pyriformis strains WH6, W, HSM, and GLC, after exposure to normal human serum, give rise to large membrane-bounded endocytic vacuoles, as visualized by transmission electron microscopy (TEM). These vacuoles do not resemble ordinary food vacuoles formed in the oral apparatus. Nor do they appear to be vacuoles containing protein concentrated from the serum: Albumin solutions induce a different type of vacuole (Brenner et al., 1976). The large bodies take a stain (PAS) that indicates the presence of polysaccharide. TEM micrographs show the presence of lipid in some of the large bodies. It is not yet known if these large body vacuoles are formed in the oral apparatus like food vacuoles or result from the fusion of pinocytic vacuoles.Although the mutant T. pyriformis strain, NP1, is unable to form a functional oral apparatus at 37° C and cannot form food vacuoles (Rasmussen and Orias, 1975), it multiplies in 2% proteose peptone medium supplemented with vitamins and heavy metal salts.

Electron Microscopy of an Intracellular Response of Tetrahymena Pyriformis to Fluids From Normal Animals

1973 ◽  
Vol 31 ◽  
pp. 578-579
Author(s):  
L. J. Brenner ◽  
D. G. Osborne ◽  
B. L. Schumaker
Keyword(s):  
Electron Microscopy ◽  
Light Microscope ◽  
Tetrahymena Pyriformis ◽  
Rabbit Serum ◽  
Small Bodies ◽  
Posterior Portion ◽  
Sudan Iv ◽  
Mouse Ascites ◽  
Normal Human ◽  
Intracellular Response

It was previously reported that log phase Tetrahymena pyriformis (strain WHg), washed free of growth medium, after mixing with normal human or rabbit serum or mouse ascites fluid, gave rise after several hours to numerous large and small bodies in the cytoplasm, as visualized by the light microscope. Generally, the large bodies remained in the posterior portion of the animal, while the small ones were localized near the anterior end. Stained preparations showed small Sudan IV positive bodies and large PAS positive bodies. Electron micrographs also identified the small bodies as lipid and showed the large ones to be enclosed within a membrane (Fig. 1) and unlike anything yet described for this organism. Whether all these large bodies correspond to the PAS positive bodies on the slide preparations is uncertain.

Surface Morphology Investigation of Poly(ether ether ketone) Immobilized with Heparin and Bovine Serum Albumin

2013 ◽  
Vol 683 ◽  
pp. 409-412
Author(s):  
Hui Sun ◽  
Rui Chao Chen ◽  
Biao Yang ◽  
Guo Zhi Xu
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Bovine Serum Albumin ◽  
Surface Morphology ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ether Ether Ketone ◽  
Poly Ether Ether Ketone ◽  
Ether Ketone ◽  
Scanning Electron

The surface topography of poly(ether ether ketone) (PEEK) film immobilized with heparin and Bovine Serum Albumin (BSA) was characterized via scanning electron microscopy (SEM). Compared with the unmodified film, the surface of modified film changed and become rough, which indirectly proved the successful introduction of monomer and biomolecule on PEEK

Studies on Characteristics and Adsorption of BSA on Hydrogel Biomaterials

2007 ◽  
Vol 330-332 ◽  
pp. 901-904
Author(s):  
G.X. Tan ◽  
Ying De Cui ◽  
Ying Jun Wang
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Chemical Stability ◽  
Contact Lens ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Radical Copolymerization ◽  
Vinyl Pyrrolidone ◽  
Equilibrium Water Content ◽  
Influence Of Ph

Hydrogel biomaterials were synthesized by radical copolymerization of N-vinyl pyrrolidone (NVP) and 2-hydroxyethylmathacrylate (HEMA), with azobisisobutyronitrile (AIBN) as an initiator, reacting at 60~70°C for 24 hours, which were designed as contact lens due to the good chemical stability and high biocompatibility. The absorbency of bovine serum albumin (BSA) was measured by the ultraviolet spectrophotometer. The influence of pH, initial protein concentration and ionic strength were investigated in detail. The results showed that the absorption of protein on hydrogel biomaterials increased with the immersing time increasing, and was stable during 4 days. The absorption of protein on hydrogel increased with the equilibrium water content increasing. The protein absorption on hydrogels reduced the permeability of the oxygen of the biomaterials.

scholarly journals Anti-Foulant Ultrafiltration Polymer Composite Membranes Incorporated with Composite Activated Carbon/Chitosan and Activated Carbon/Thiolated Chitosan with Enhanced Hydrophilicity

Membranes ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 827
Author(s):  
Syeda Samia Nayab ◽  
M. Asad Abbas ◽  
Shehla Mushtaq ◽  
Bilal Khan Niazi ◽  
Mehwish Batool ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Contact Angle ◽  
Activated Carbon ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Carbon Composite ◽  
Flux Rate ◽  
Thiolated Chitosan ◽  
Scanning Electron

A rapid increase in population worldwide is giving rise to the severe problem of safe drinking water availability, necessitating the search for solutions that are effective and economical. For this purpose, membrane technology has shown a lot of promise but faces the challenge of fouling, leading to a reduction in its lifetime. In this study, ultrafiltration polyethersulfone membranes were synthesized in two different concentrations, 16% wt. and 20% wt., using the phase inversion method. Chitosan and activated carbon were incorporated as individual fillers and then as composites in both the concentrations. A novel thiolated chitosan/activated carbon composite was introduced into a polyethersulfone membrane matrix. The membranes were then analyzed using Attenuated Total Reflection–Fourier-Transform Infrared spectroscopy (ATR-FTIR), Scanning Electron Microscopy (SEM), optical profilometry, gravimetric analysis, water retention, mechanical testing and contact angle. For membranes with the novel thiolated chitosan/activated carbon composite, Scanning Electron Microscopy micrographs showed better channels, indicating a better permeability possibility, reiterated by the flux rate results. The flux rate and bovine serum albumin flux were also assessed, and the results showed an increase from 105 L/m2h to 114 L/m2h for water flux and the antifouling determined by bovine serum albumin flux increased from 23 L/m2h to 51 L/m2h. The increase in values of water uptake from 22.84% to 76.5% and decrease in contact angle from 64.5 to 55.7 showed a significant increase in the hydrophilic character of the membrane.

scholarly journals The role of monocytes in serum sickness nephritis.

1979 ◽  
Vol 150 (3) ◽  
pp. 413-425 ◽  
Author(s):  
L G Hunsicker ◽  
T P Shearer ◽  
S B Plattner ◽  
D Weisenburger
Keyword(s):  
Electron Microscopy ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
The Other ◽  
Serum Sickness ◽  
Nonspecific Esterase ◽  
Immune Clearance ◽  
Rate Of Increase ◽  
Serum Sickness Nephritis

We have investigated the pathogenesis of glomerular hypercellularity seen in acute serum sickness nephritis induced in rabbits with bovine serum albumin (BSA). The increase in cellularity began with the first stages of immune clearance of BSA, with a peak cellularity occuring at the time of onset of proteinuria. Although there was a significant increase in the fraction of glomerular cells incorporating [3H]thymidine, first seen at the onset of proteinuria, this increase occurred too late and was too small to explain the observed rate of increase in glomerular cellularity. On the other hand, a striking monocytic infiltration of the glomeruli was documented by electron microscopy and by staining for nonspecific esterase. This monocytic infiltration paralleled the observed course of glomerular hypercellularity and was quantitatively sufficient to explain the total increase seen. It appears, therefore, that glomerular hypercellularity seen in this model is principally a result of monocyte infiltration.

scholarly journals Efficacy of alcohol/sugar aqueous biphasic system on partition of bovine serum albumin

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Yin Hui Chow ◽  
Alagan Sahlini ◽  
Hui-Suan Ng ◽  
John Chi-Wei Lan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Protein Extraction ◽  
Ftir Analysis ◽  
Model Protein ◽  
Aqueous Biphasic ◽  
The Fourier Transform ◽  
Protein Bovine Serum Albumin

AbstractThe efficacy of alcohol/sugar aqueous biphasic (ABS) system on protein extraction was investigated. A model protein, bovine serum albumin (BSA), was adopted to evaluate the effects of types and concentration of phase-forming components, protein concentration, and system pH on the protein partition efficiency. The 1-propanol/maltose ABS exhibited an overall better partition efficiency of BSA to the alcohol-rich top phase. A maximum partition coefficient (K) of 20.01 ± 0.05 and recovery yield (Y) of 95.42% ± 0.01% of BSA were achieved with 35% (w/w) 1-propanol/22% (w/w) maltose ABS at pH 5.0 for 10% (w/w) BSA load. The K and Y of BSA in 1-propanol/maltose ABS was slightly improved with the addition of 3% (w/w) of ionic liquid, 1-butyl-3-methylimidazolium bromide ([Bmim]Br) as the adjuvant that could provide protein stabilizing effect. The Fourier Transform Infrared Spectrum (FTIR) analysis revealed that the protein structure remained unaltered upon the separation process.

scholarly journals Effect of protein-tannin ratio and tannin concentration on the bovine serum albumin (BSA)-based precipitation method for red wine tannin concentration

OENO One ◽  
2011 ◽  
Vol 45 (1) ◽  
pp. 39
Author(s):  
Belinda S. Kemp ◽  
Roland Harrison ◽  
Richard N. Hider
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Red Wine ◽  
Ethanol Concentration ◽  
Precipitation Method ◽  
Red Wines ◽  
Protein Ratio ◽  
Tannin Concentration

<p style="text-align: justify;"><strong>Aims</strong>: The main objective of the study was to ascertain whether an existing protein precipitation assay could be simply modified to determine tannin at low concentration in wines. This was achieved by mixing a greater volume of wine to a smaller, but more concentrated, volume of bovine serum albumin (BSA) to maintain the same wine-to-BSA ratio (although both the final pH and ethanol concentration varied). In addition, dilution series of each of these mixtures were prepared to investigate the effect of wine-to-BSA ratio on tannin precipitation.</p><p style="text-align: justify;"><strong>Methods and results</strong>: Seven New Zealand red wines were assayed according to the BSA method using a range of protein (BSA) and wine concentrations achieved by varying wine dilutions and the volume of the model wine solution. Maximum precipitation was observed at lower wine/protein ratios in diluted wines and tannin precipitation increased as protein concentration increased. It was observed that the estimation of tannin concentration in red wine is a product of tannin/protein ratio and BSA concentration. Consequently, the methylcellulose precipitation (MCP) assay was performed to independently determine tannin concentration in red wines. Results indicate that tannin/protein ratio, BSA concentration and possibly tannin composition affect BSA-tannin precipitation.</p><p style="text-align: justify;"><strong>Conclusion</strong>: For the BSA assay there appears to be a region of low tannin/protein ratio within which lower wine tannin concentrations can be determined. Overall it is suggested that tannin precipitation is linearly related to tannin concentration.</p><p style="text-align: justify;"><strong>Significance and impact of the study</strong>: Results showed the limits of the BSA method for low tannin wines and the difficulty in using the method for wines with unknown tannin concentrations.</p>

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