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.

scholarly journals The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

1980 ◽  
Vol 189 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Yoav Ben-Yoseph ◽  
Melinda Hungerford ◽  
Henry L. Nadler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Krabbe Disease ◽  
Low Molecular Weight ◽  
Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

scholarly journals High Molecular Weight Factor VIII Coagulant Activity in Cryoprecipitate and Polyethylene Glycol Precipitates

1977 ◽  
Author(s):  
K. A. Rickard ◽  
T. Exner ◽  
H. Kronenberg
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Factor Viii ◽  
High Molecular Weight ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Human Antibody ◽  
High Molecular Weight Material ◽  
Coagulant Activity ◽  
Molecular Weight Form

Gel filtration of human plasma cryoprecipitate on Sepharose 2B indicated the molecular weight of factor VIII coagulant activity (VIIIc) to be significantly greater than that found in antihaemophilic concentrate. Polyethylene glycol at 3% concentration precipitated approximately half of the VIIIc from cryoprecipitate. This activity eluted as high molecular weight material on gel filtration. The addition of more polyethylene glycol to a concentration of 8% precipitated most of the remaining VIIIc from cryoprecipitate. This activity appeared to be of significantly lower molecular weight, approximately corresponding in elution volume to that observed for antihaemophilic concentrate. The possibility that an antibody to VIIIc generated in a patient treated with cryoprecipitate might be directed against the higher molecular weight form of factor VIII was investigated. However, no significant differences between the higher and lower molecular weight forms of factor VIII either in stability or in reactivity with human antibody to factor VIII were found.

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.

Immunoaffinity Chromatography of Canine High-Molecular-Weight Renin: Partial Purification and Characterization

1983 ◽  
Vol 65 (2) ◽  
pp. 117-120 ◽  
Author(s):  
Fumihiko Ikemoto ◽  
Victor J. Dzau ◽  
Edgar Haber ◽  
Kazuo Takaori ◽  
Kenjiro Yamamoto
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Immunoaffinity Chromatography ◽  
Partial Purification ◽  
Low Molecular Weight ◽  
Specific Method ◽  
Disulphide Bonds ◽  
Binding Substance ◽  
Molecular Weight Form

1. Canine high-molecular-weight renin (mol. wt. 60 000) is believed to be a complex of renin (low-molecular-weight form, mol. wt. 40 000) and renin-binding substance. The immunocross-reactivity of high-molecular-weight renin and low-molecular-weight renin was demonstrated by using antibodies specific to low-molecular-weight renin. 2. Immunoaffinity chromatography with renin-specific antibodies coupled to Sepharose provided a simple and specific method for isolation of high-molecular-weight renin. High-molecular-weight renin with a specific activity of 137 600 ng of ANG I h−1 mg−1 of protein (19.6 Goldblatt units/mg of protein) was obtained. 3. This high-molecular-weight renin was stable in dithiothreitol (25 mmol/l), suggesting that disulphide bonds may not be involved in the binding mechanism between low-molecular-weight renin and renin-binding substance. 4. However, exposure to low pH (3.0) resulted in conversion of high-molecular-weight renin into the low-molecular-weight form.

scholarly journals Digestion of the zinc in human milk, cow's milk and a commercial babyfood: some implications for human infant nutrition

1986 ◽  
Vol 55 (2) ◽  
pp. 209-217 ◽  
Author(s):  
Peter Blakeborough ◽  
Michael I. Gurr ◽  
Dallyn N. Salter
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight ◽  
Stomach Contents ◽  
Human Infant ◽  
Soluble Form ◽  
Cow’S Milk ◽  
Low Molecular Weight ◽  
Cow's Milk ◽  
Molecular Weight Form

1. The digestion of zinc present in human milk, cow's milk and a commercial babyfood was compared, using the piglet as a model for the human infant.2. In piglets given human milk the pH of stomach contents was approximately 1 and 0.4 units lower than that of animals given respectively cow's milk and babyfood. The pH values of intestinal contents were approximately neutral and did not vary with the type of feed.3. Hard casein curds were present throughout the stomachs and small intestines of animals fed on cow's milk or babyfood and between 55 and 70% Zn in these digesta samples were recovered in an insoluble form by centrifugation. In contrast, little solid material was observed in the digesta of animals fed on human milk, and 57 and 93% respectively of the Zn in digesta were recovered in a soluble form in the stomach and small intestine.4. Soluble fractions prepared by centrifugation of digesta were analysed by filtration on Sephadex G-150. After any of the three feeds, soluble Zn in stomach contents was mainly in a low-molecular-weight form. In intestinal samples, however, Zn was present in low- and high-molecular-weight forms. Whilst there were similar amounts of Zn in the low-molecular-weight form in all samples, approximately three times as much of the total intestinal Zn was in a soluble high-molecular-weight form complexed to proteins in the animals fed on human milk compared with those fed on cow's milk or babyfood.5. Analysis of protein-bound soluble Zn in intestinal samples on SDS-polyacrylamide gels resulted in a similar pattern of proteins for all feeds. Results indicated that at least some of these proteins were derived from intestinal secretions of the piglet.6. Some implications of these results in respect of the mode of digestion of Zn and its biological availability to the human infant are discussed.

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.

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.

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