scholarly journals Structural proteins of plasmolemma of the jejunum absorbing enterocytes of cattle fetus in early fetal period

2019 ◽  
Vol 2 (3) ◽  
pp. 32-38
Author(s):  
D. M. Masiuk
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Basolateral Membrane ◽  
Protein Fractions ◽  
Low Molecular Weight ◽  
Fetal Period ◽  
Basolateral Membranes ◽  
Molecular Weights ◽  
Early Fetal Period ◽  
Apical Membranes

The data on the concentration of structural proteins of plasmolemma of the absorption enterocytes of the cattle fetus in the early fetal period are presented. Changes in the protein composition of the apical and basolateral membranes of enterocytes are manifested, characterized not only by changes in their ratio within different cell domains, but also by the dynamic redistribution of the number of different fractions of polypeptides between the poles of these cells. Analysis of the results of electrophoresis of apical membranes of the cattle fetus enterocytes in the early fetal period indicates a decrease in the content of low molecular weight protein fractions and an increase in high molecular weight. In the apical membranes of enterocytes of two-month-old cattle fetus, 25 protein fractions with a molecular weight of 9.6 to 205 kDa were detected. In the basolateral membranes revealed 23 protein fractions with a molecular weight of 9.6 to 120 kDa. High molecular weight fractions of polypeptides with molecular weights of 250 kDa and 300 kDa appear from the age of three months of embryos of calves. In the basolateral membranes of enterocytes, there is a slight decrease in the content of low molecular weight protein fractions, and from the four months of age of cattle fetus, high molecular weight fractions of polypeptides with molecular weights of 22.5 kDa and 155 kDa appear, which are absent in basolateral membranes of enterocytes. Two-month-old fetus lack proteins with a molecular weight of 19 kDa, 24 kDa, and 66 kDa in the apical part, whereas proteins with a mass of 22.5 kDa, 155 kDa, 170–185 kDa, and 205 kDa are absent on the basolateral membrane. In the apical membrane of enterocytes significantly more proteins with a low molecular weight of 9.6-14.2 kDa (1.56 times; P ≤ 0.001), whereas in the basolateral membrane a significantly higher concentration of proteins with a molecular weight of 15.5 kDa (2.06 times; P ≤ 0.001) and 17 kDa (3.62 times; P ≤ 0.001).

scholarly journals Structural proteins of plasmolemma of the jejunum absorbing enterocytes of cattle fetus in early fetal period

2019 ◽  
Vol 2 (3) ◽  
pp. 32-38
Author(s):  
D. M. Masiuk
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Basolateral Membrane ◽  
Protein Fractions ◽  
Low Molecular Weight ◽  
Fetal Period ◽  
Basolateral Membranes ◽  
Molecular Weights ◽  
Early Fetal Period ◽  
Apical Membranes

The data on the concentration of structural proteins of plasmolemma of the absorption enterocytes of the cattle fetus in the early fetal period are presented. Changes in the protein composition of the apical and basolateral membranes of enterocytes are manifested, characterized not only by changes in their ratio within different cell domains, but also by the dynamic redistribution of the number of different fractions of polypeptides between the poles of these cells. Analysis of the results of electrophoresis of apical membranes of the cattle fetus enterocytes in the early fetal period indicates a decrease in the content of low molecular weight protein fractions and an increase in high molecular weight. In the apical membranes of enterocytes of two-month-old cattle fetus, 25 protein fractions with a molecular weight of 9.6 to 205 kDa were detected. In the basolateral membranes revealed 23 protein fractions with a molecular weight of 9.6 to 120 kDa. High molecular weight fractions of polypeptides with molecular weights of 250 kDa and 300 kDa appear from the age of three months of embryos of calves. In the basolateral membranes of enterocytes, there is a slight decrease in the content of low molecular weight protein fractions, and from the four months of age of cattle fetus, high molecular weight fractions of polypeptides with molecular weights of 22.5 kDa and 155 kDa appear, which are absent in basolateral membranes of enterocytes. Two-month-old fetus lack proteins with a molecular weight of 19 kDa, 24 kDa, and 66 kDa in the apical part, whereas proteins with a mass of 22.5 kDa, 155 kDa, 170–185 kDa, and 205 kDa are absent on the basolateral membrane. In the apical membrane of enterocytes significantly more proteins with a low molecular weight of 9.6-14.2 kDa (1.56 times; P ≤ 0.001), whereas in the basolateral membrane a significantly higher concentration of proteins with a molecular weight of 15.5 kDa (2.06 times; P ≤ 0.001) and 17 kDa (3.62 times; P ≤ 0.001).

scholarly journals Expression of plasmolemma proteins of the absorptive enterocytes of the cattle in the late fetal period

2020 ◽  
Vol 3 (1) ◽  
pp. 52-57
Author(s):  
D. M. Masiuk
Keyword(s):  
Molecular Weight ◽  
Basolateral Membrane ◽  
Protein Fractions ◽  
Low Molecular Weight ◽  
Fetal Period ◽  
Molecular Weights ◽  
Weight Protein ◽  
Low Molecular Weight Protein ◽  
Apical Membranes ◽  
Absorptive Enterocytes

The article presents new scientific data on the expression of plasmalemma proteins of the absorptive enterocytes of the bovine intestines of five to nine months of age. In the late fetal period, 31 and 27 protein fractions of apical and basolateral membranes, respectively, were found in the plasmalemma of the jejunum intestine, which had a molecular weight of 9.6 kDa to 300 kDa. Twenty-nine protein fractions were detected in the apical membranes of five-month-old cattle enterocytes. It should be noted that protein fractions with low molecular weight (up to 24 kDa) were only 19.7 %, with molecular weights from 24 kDa to 100 kDa – 69.2 %, and fractions with molecular weights of 100 kDa and more were detected only – 11.1 % of the total number of polypeptides. Twenty-five protein fractions with a molecular weight of 9.6 to 155 kDa were found in the basolateral enterocyte membranes of five-month-old fetus. A large proportion of the detected protein fractions belonged to low molecular weight polypeptides (9.6–24 kDa – 40.26 %). Proteins with a molecular weight of 24–95 kDa – 55.2 %, with a molecular mass of 100 kDa and more were found only 4.56 %. High molecular weight proteins in the basolateral membrane of jejunum enterocytes of five-months-old cattle with a molecular weight greater than 155 kDa were not detected by electrophoresis (unlike the apical membrane). Analysis of the results of studies membranes protein of cattle enterocytes in late fetal period indicates significant changes in their polypeptide composition. In particular, in the basolateral membranes of enterocytes during the late fetal period there is a decrease in the content of low molecular weight protein fractions (3.3 times; P ≤ 0.001) and an increase in the proportion of high molecular weight. In addition, from the age of eight months, proteins with a molecular weight of 9.6–14.2 kDa and 75 kDa disappear in the basolateral membrane. Instead, proteins with a molecular weight of 300 kDa and 170-1885 kDa are appeared. In addition, in the apical membranes of enterocytes there is a significant decrease in the content of low molecular weight protein fractions and an increase in polypeptides with a molecular weight greater than 100 kDa. The appearance in the apical membranes of jejunum enterocytes of calves from eight months of age embryonic development of fractions of polypeptides with molecular weight of 24 kDa and 66 kDa, which are present until the end of the fetal period.

scholarly journals Biodegradation of low molecular weight polyacrylamide under aerobic and anaerobic conditions: effect of the molecular weight

2020 ◽  
Vol 81 (2) ◽  
pp. 301-308 ◽  
Author(s):  
Wenzhe Song ◽  
Yu Zhang ◽  
Amir Hossein Hamidian ◽  
Min Yang
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Carbon Chain ◽  
Anaerobic Treatment ◽  
Low Molecular Weight ◽  
Amino Groups ◽  
Molecular Weights ◽  
Weight One ◽  
Hydrolysis Of ◽  
Aerobic And Anaerobic

Abstract The biodegradation of polyacrylamide (PAM) includes the hydrolysis of amino groups and cleavage of the carbon chain; however, the effect of molecular weight on the biodegradation needs further investigations. In this study, biodegradation of low molecular weight PAM (1.6 × 106 Da) was evaluated in two aerobic (25 °C and 40 °C) and two anaerobic (35 °C and 55 °C) reactors over 100 days. The removal of the low molecular weight PAM (52.0–52.6%) through the hydrolysis of amino groups by anaerobic treatment (35 °C and 55 °C) was much higher than that of the high molecular weight (2.2 × 107 Da, 11.2–17.0%) observed under the same conditions. The molecular weight was reduced from 1.6 × 106 to 6.45–7.42 × 105 Da for the low molecular weight PAM, while the high molecular weight PAM declined from 2.2 × 107 to 3.76–5.87 × 106 Da. The results showed that the amino hydrolysis of low molecular weight PAM is easier than that of the high molecular weight one, while the cleavage of its carbon chain is still difficult. The molecular weights of PAM in the effluents from the two aerobic reactors (25 °C and 40 °C) were further reduced to 4.31 × 105 and 5.68 × 105 Da by the biofilm treatment, respectively. The results would be useful for the management of wastewater containing PAM.

scholarly journals Effects Of Environmental Factors On The Dispersion Behavior Of Iron Oxide In Aqueous Solutions With Poly Acrylic Acid

2015 ◽  
Vol 60 (2) ◽  
pp. 1561-1564
Author(s):  
E.-H. Lee ◽  
K.-M. Kim ◽  
W.-Y. Maeng ◽  
D.-H. Hur
Keyword(s):  
Molecular Weight ◽  
Acrylic Acid ◽  
High Molecular Weight ◽  
Low Molecular Weight ◽  
Solution Ph ◽  
Molecular Weights ◽  
Aqueous Suspensions ◽  
Magnetite Particles ◽  
The Stability ◽  
Poly Acrylic Acid

Abstract After preparing aqueous suspensions from magnetite particles with a poly-acrylic acid, we investigated the effects of several experimental parameters. We characterized the stability of the suspensions using visual inspection, sedimentation, adsorption, and thermal stability of the dispersant. The dispersion stability is affected by the solution pH, the concentrations of magnetite particles, the molecular weight, the concentration of the dispersants, and the temperature. The stability of the suspensions increased as the concentration of the dispersant and the temperature increased. In terms of the molecular weights of the dispersant, the suspensions with dispersant of low-molecular weight (1800) were more stable than those of high-molecular weight (250000) at room temperature. However, at high temperature the suspensions with high-molecular weight showed stability. The adsorption efficiency of the dispersant was very low. The dispersant of high-molecular weight showed a higher thermal integrity than that of low-molecular weight. From this work, we obtained the optimum conditions for stable aqueous suspensions of magnetite particles.

scholarly journals The morphological changes relationship in the small intestine mucous membrane with the dynamics of the enterocyte’s membranes polypeptide composition in cattle during the fetal period of their ontogenesis

2021 ◽  
Vol 9 (1) ◽  
pp. 52-56
Author(s):  
D. M. Masiuk
Keyword(s):  
Molecular Weight ◽  
Mucous Membrane ◽  
Apical Membrane ◽  
Morphological Changes ◽  
Basolateral Membrane ◽  
Intestinal Wall ◽  
Current Data ◽  
Polypeptide Composition ◽  
Fetal Period ◽  
Molecular Weights

The article presents current data on the relationship of morphological changes in the jejenum intestine mucous membrane with the dynamics of the polypeptide composition in the cattle enterocytes membranes during the fetal period of ontogenesis. The study was carried out on 80 fetuses of Holstein cattle, aged 2–9 months, with a body weight of 0.6–39 kg. It was found that during the fetal period of ontogenesis, structural transformations took place in the jejunal mucous membrane of cattle, characterized by intense morphofunctional changes in its structural components. The polypeptide composition of the jejunal enterocytes plasma membrane in cattle during the fetal period of ontogenesis was determined, in particular, in the apical and basolateral membranes, respectively, 27 and 25 protein fractions with a molecular weight of 9.6–14.2 kDa to 300 kDa were found, respectively. With the help of the correlation analysis for the received data, reliable interconnections of morphological changes in the jejunal mucous layer with the dynamics of the polypeptide composition of the cattle enterocyte’s membranes during the fetal period of ontogenesis were obtained. It has been proven that the thickness of the intestinal wall with villi and the mucous membrane with villi is directly related to the content of proteins with a molecular weight of 250 kDa and 155 kDa on the apical domain of enterocytes (P ≤ 0.01–0.001). The height of the villi is associated only with the content of polypeptides with a molecular weight of 250 kDa and 155 kDa (P ≤ 0.05–001) in the apical membrane and is inversely related to the content of polypeptides with a molecular weight of 9.6–14.2 kDa, 21 kDa, 22.5 kDa, 26 kDa, 33 kDa, 35 kDa, 170–185 kDa (P ≤ 0.01–0.001). The width of the villi is related to the content on the apical membrane of proteins with a molecular weight of 170–185 kDa and 21 kDa (P ≤ 0.05–0.01). The thickness of the intestinal wall with villi and mucous membrane with villi is associated with the content of proteins with molecular weights 155 kDa, 100 kDa, 87 kDa, 66 kDa, 52 kDa) and 43 kDa (P ≤ 0.05–0.001) on the basolateral domain of enterocytes and inversely dependent on the content of polypeptides with molecular weights of 19 kDa, 21 kDa and 31 kDa (P ≤ 0.05). The height of enterocyte villi is directly related to the content of polypeptides with a molecular weight of 155 kDa and 52 kDa (P ≤ 0,05–0,01) in the basolateral membrane and is inversely dependent on the content of polypeptides with a molecular weight of 24 kDa, 22.5 kDa and 17 kDa (P ≤ 0.05–0.001). The width of the villi of enterocytes is reliably inversely related only to the content of proteins with a molecular weight of 155 kDa on the basolateral membrane (P ≤ 0.05).

Analysis of proteins in rabbit pulmonary surfactant using monoclonal antibodies

1986 ◽  
Vol 250 (3) ◽  
pp. C460-C467 ◽  
Author(s):  
R. J. King ◽  
H. M. Martin ◽  
J. B. Baseman ◽  
J. Morrison-Plummer
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Pulmonary Surfactant ◽  
Polyacrylamide Gel Electrophoresis ◽  
Low Molecular Weight ◽  
Weight Group ◽  
Molecular Weights ◽  
Intermediate Group

We have used monoclonal antibodies developed against the apolipoproteins associated with pulmonary surfactant purified from rabbit lavage fluid to study the expression of epitopes common to these proteins. The pulmonary surfactant contained nearly 20 proteins, of which at least 10 were not derived from serum. Electrophoresis, with sulfhydryl reduction of these proteins indicated apparent molecular weights of approximately 155, 135, 125, and 115 X 10(3) (high-molecular-weight group); 80, 70, and 60 X 10(3) (intermediate group); and 18 through 10 X 10(3) (low-molecular-weight group). Two-dimensional polyacrylamide gel electrophoresis, in which the proteins were electrophoresed without reduction in the first dimension, but with sulfhydryl reduction in the second dimension, revealed that the 80, 70, and 60 X 10(3) proteins dissociated into proteins of nominal molecular weights of 40, 35, and 30 X 10(3), respectively. In contrast, the 125 and 115 X 10(3) proteins of the high-molecular-weight group contained a protein which could only be reduced to a minimum molecular weight of 55 to 60 X 10(3). Monoclonal antibodies generally were of three types: those that reacted strongly with the high-molecular-weight group and weakly with the intermediate group; those that reacted conversely; and those that reacted only with the low-molecular-weight group. Our results indicate that at least two different surfactant apolipoproteins, with differing minimum molecular weights in SDS-polyacrylamide gel electrophoresis, have common epitopes. Although these results cannot certify a physiological relationship between these proteins, they suggest that the intracellular synthesis or extracellular processing of surfactant apolipoproteins may be more complicated than predicted by the findings of previous experiments, perhaps involving the posttranslational assembly of one surfactant protein into oligomers which resist dissociation under the conditions used for the analyses.

Conditions Affecting the Molecular Weight of Factor VIII.

1979 ◽  
Author(s):  
G. Rock ◽  
E. Tackaberry ◽  
D. Palmer
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
High Molecular Weight ◽  
Calcium Concentration ◽  
Low Molecular Weight ◽  
Biochemical Purification ◽  
Molecular Weights ◽  
Will Self ◽  
And Storage ◽  
Molecular Weight Form

By purifying Factor VIII while maintaining physiological concentrations of calcium we have recently demonstrated that about 50% of the procoagulant activity is in a very low molecular weight (VLHW) form not associated with the carrier (VIII: RAG). The remainder is carrier associated and elutes at Vo as a high molecular weight (HMW) compound upon Sepharose 6B chromatography. Reduction of the calcium concentration by increasing the amount of citrate added to heparin results in decreasing the ratio of VLMW:HMW from 1:1 in pure heparin to 1:5 in pure citrate. If citrate is replaced with the more strongly chelating EDTA no VLMW is detectable in the plasma. It has also been found that most of the biochemical purification techniques which have been previously used to prepare Factor VIII for study actually result in the aggregation of this VLMW with the carrier to produce the high molecular weight form. This includes: cryoprecipitation, precipitation by polyethylene glycol and storage -80°C. As well, the VLMW material will self-associate upon freezing to produce an aggregate with a molecular weight of 106. However, this material does not cross-react with rabbit antibody directed against VIII: RAG. The data indicate that many of the previously reported biochemical characteristics, including molecular weights, actually describe species which are artifacts of the isolation process rather than those of the physiologically occuring Factor VIII.

Experimental Study on Flow-Front Fingering Instabilities in Injection Molding of Polymer Solutions and Melts

2004 ◽  
Author(s):  
Kalonji K. Kabanemi ◽  
Jean-Franc¸ois He´tu ◽  
Samira H. Sammoun
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Polymer Solutions ◽  
Low Molecular Weight ◽  
Flow Front ◽  
High Molecular Weight Polymer ◽  
Molecular Weight Polymer ◽  
Polymer Molecules ◽  
Molecular Weights ◽  
Solvent Molecules

An experimental investigation of the flow behavior of dilute, semi-dilute and concentrated polymer solutions has been carried out to gain a better understanding of the underlying mechanisms leading to the occurrence of instabilities at the advancing flow front during the filling of a mold cavity. Experiments were performed using various mass concentrations of low and high molecular weight polyacrylamide polymers in corn syrup and water. This paper reports a new type of elastic fingering instabilities at the advancing flow front that has been observed only in semi-dilute polymer solutions of high molecular weight polymers. These flow front elastic instabilities seem to arise as a result of a mixture of widely separated high molecular weight polymer molecules and low molecular weight solvent molecules, which gives rise to a largely non-uniform polydisperse solution, with respect to all the kinds of molecules in the resulting mixture (solvent molecules and polymer molecules). The occurrence of these instabilities appears to be independent of the injection flow rate and the cavity thickness. Moreover, these instabilities do not manifest themselves in dilute or concentrated regimes, where respectively, polymer molecules and solvent molecules are minor perturbation of the resulting solution. In those regimes, smooth flow fronts are confirmed from our experiments. Based on these findings, the experimental investigations have been extended to polymer melts. Different mixtures of polycarbonate melts of widely separated molecular weights (low and high molecular weights) were first prepared. The effect of the large polydispersity of the resulting mixtures on the flow front behavior was subsequently studied. The same instabilities at the flow front were observed only in the experiments where a very small amount of high molecular weight polycarbonate polymer has been mixed to a low molecular weight polycarbonate melt (oligomers).

scholarly journals Fire Resistance, Thermal and Anti-Ageing Properties of Transparent Fire-Retardant Coatings Modified with Different Molecular Weights of Polyethylene Glycol Borate

Polymers ◽  
2021 ◽  
Vol 13 (23) ◽  
pp. 4206
Author(s):  
Long Yan ◽  
Xinyu Tang ◽  
Xiaojiang Xie ◽  
Zhisheng Xu
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
High Molecular Weight ◽  
Fire Resistance ◽  
Fire Retardant ◽  
Phosphate Ester ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Flame Retarded ◽  
Residual Weight

Four kinds of polyethylene glycol borate (PEG-BA) with different molecular weights were grafted into cyclic phosphate ester (PEA) to obtain flexible phosphate esters (PPBs), and then applied in amino resin to obtain a series of transparent intumescent fire-retardant coatings. The comprehensive properties of the transparent coatings containing different molecular weights of PEG-BA were investigated by various analytical instruments. The transparency and mechanical analyses indicate that the presence of PEG-BA slightly decreases the optical transparency of the coatings but improves the flexibility and adhesion classification of the coatings. The results from fire protection and cone calorimeter tests show that low molecular weight of PEG-BA exerts a positive flame-retarded effect in the coatings, while high molecular weight of PEG800-BA behaves against flame-retarded effect. Thermogravimetric and char residue analyses show that the incorporation of low molecular weight of PEG-BA clearly increases the thermal stability and residual weight of the coatings and generates a more compact and stable intumescent char on the surface of the coatings, thus resulting in superior synergistic flame-retarded effect. In particular, MPPB1 coating containing PEG200-BA exerts the best flame-retarded effect and highest residual weight of 36.3% at 700 °C, which has 57.6% reduction in flame spread rate and 23.9% reduction in total heat release compared to those of MPPB0 without PEG-BA. Accelerated ageing test shows that low molecular weight of PEG-BA promotes to enhance the durability of structural stability and fire resistance of the coatings, while PEG800-BA with high molecular weight weakens the ageing resistance. In summary, the fire-resistant and anti-ageing efficiencies of PEG-BA in the coatings depend on its molecular weight, which present the order of PEG200-BA > PEG400-BA > PEG600-BA > PEG800-BA.

Variability of Low-Molecular-Weight, Heat-Modifiable Outer Membrane Proteins of Neisseria meningitidis

1980 ◽  
Vol 30 (3) ◽  
pp. 642-648
Author(s):  
J. T. Poolman ◽  
S. De Marie ◽  
H. C. Zanen
Keyword(s):  
Molecular Weight ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Sds Page ◽  
Index Cases

Analysis of major outer membrane protein (MOMP) profiles of various meningococci by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of 0 to 2 low-molecular-weight, heat-modifiable MOMPs (molecular weight, 25,000 to 32,000) and 1 to 3 high-molecular-weight MOMPs (molecular weight, 32,000 to 46,000). Heat modifiability was investigated by comparing MOMP profiles after heating in SDS solutions at 100°C for 5 min or at 40°C for 1 h. Low-molecular-weight MOMPs shifted to higher apparent molecular weights after being heated at 100°C. Heat modifiability of high-molecular-weight MOMPs varied among strains; whenever modified these proteins shifted to lower apparent molecular weights after complete denaturation. Variability of low-molecular-weight, heat-modifiable MOMPs was demonstrated when MOMP profiles were compared of (i) isolates from index cases and associated cases and carriers among contacts, (ii) different isolates from the same individual, and (iii) isolates from a small epidemic caused by serogroup W-135. In some cases high-molecular-weight MOMPs revealed quantitative differences among related strains. The observed variability and quantitative differences indicate that MOMP serotyping and typing on the basis of SDS-PAGE profiles (PAGE typing) need careful reevaluation.

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