scholarly journals Studies on the Apoproteins of the Major Lipoprotein of the Yolk of Hen's Eggs III. Influence of Salt Concentration During Isolation on the Amount and Composition of the Apoproteins

1978 ◽  
Vol 31 (6) ◽  
pp. 587 ◽  
Author(s):  
RW Burley
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Aqueous Phase ◽  
Salt Concentration ◽  
High Salt ◽  
Salt Solutions

When the major lipoprotein of hen's eggs was prepared by centrifuging yolk in salt solutions, the ionic strength affected the apoprotein mixture. At high salt concentrations (ionic strength above about 2) more protein was present in the lipoprotein than at lower ionic strength. The extra protein was not removed by subsequently lowering the ionic strength. This extra protein consisted largely of proteins of high molecular weight, including, according to electrophoresis, y-livetin from the aqueous phase of yolk.

scholarly journals The multiple complexes formed by the interaction of platelet factor 4 with heparin

1980 ◽  
Vol 191 (3) ◽  
pp. 769-776 ◽  
Author(s):  
P E Bock ◽  
M Luscombe ◽  
S E Marshall ◽  
D S Pepper ◽  
J J Holbrook
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Chain Length ◽  
Salt Concentration ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
High Protein ◽  
Platelet Factor ◽  
The Stability ◽  
Very High

The anisotropy of the fluorescence of dansyl (5-dimethylaminonaphthalene-1- sulphonyl) groups covalently attached to human platelet factor 4 was used to detect the macromolecular compounds formed when the factor was mixed with heparin. At low heparin/protein ratios a very-high-molecular-weight compound (1) was formed that dissociated to give a smaller compound (2) when excess heparin was added. 2. A large complex was also detected as a precipitate that formed at high protein concentrations in chloride buffer. It contained 15.7% (w/w) polysaccharide, equivalent to four or five heparin tetrasaccharide units per protein tetramer. In this complex, more than one molecule of protein binds to each heparin molecule of molecular weight greater than about 6 × 10(3).3. The stability of these complexes varied with pH, salt concentration and the chain length of the heparin. The limit complexes found in excess of the larger heparins consisted of only one heparin molecule per protein tetramer, and the failure to observe complexes with four heparin molecules/protein tetramer is discussed.

The Micromorphology of Anionic Polyacrylamide Dispersions

2011 ◽  
Vol 396-398 ◽  
pp. 2310-2313
Author(s):  
Jiao Lu ◽  
Xiang Chen Fang ◽  
An Jie Wang ◽  
Xi Wen Zhang ◽  
Bo Peng
Keyword(s):  
Molecular Weight ◽  
Salt Concentration ◽  
Particle Shape ◽  
Dispersion Polymerization ◽  
Salt Solutions ◽  
Reaction Conditions ◽  
Aqueous Salt Solutions ◽  
Anionic Polyacrylamide

Anionic polyacrylamide dispersions were prepared by dispersion polymerization in aqueous salt solutions. The effects of reaction conditions, such as salt concentration, molecular weight of stabilizers, on the micromorphology of the dispersions were investigated systematically by using biological photomicroscope. The results showed that the particle shape in stable dispersions were more regular, basically spherical or ellipsoidal. Stable anionic polyacrylamide dispersions could be obtained on condition that salt concentration was between 26%~30%, molecular weight of stabilizers between 1.760×106~2.317×106 g•mol-1.

Dispersion Polymerization of Acrylamide and Acrylic Acid in Aqueous Media

2009 ◽  
Vol 87-88 ◽  
pp. 233-238
Author(s):  
Jiao Lu ◽  
Bo Peng ◽  
Ming Yuan Li ◽  
Mei Qin Lin
Keyword(s):  
Aqueous Solution ◽  
Molecular Weight ◽  
Acrylic Acid ◽  
Intrinsic Viscosity ◽  
Salt Concentration ◽  
Apparent Viscosity ◽  
Dispersion Polymerization ◽  
Aqueous Media ◽  
Salt Solutions ◽  
Aqueous Salt Solutions

Dispersion polymerization of acrylamide and acrylic acid was successfully carried out in aqueous salt solutions using anionic polyelectrolytes as stabilizers. The influences of aqueous solution of salt concentration, molecular weight and concentration of the stabilizers on the apparent viscosity and stability of the dispersions, and on the molecular weight of the polymers prepared were investigated. The results showed that stable dispersions could be obtained on condition that salt concentration was between 26%~30%, concentration of stabilizers between 8%~12%, and intrinsic viscosity of stabilizers between 2.977~3.740 dL/g. With salt concentration ranging from 26% to 30%, molecular weight of products increased first and then decreased. Molecular weight of products was hardly changed when concentration of stabilizer was between 8%~12%. When intrinsic viscosity of stabilizer was between 2.977~3.740 dL/g, increase of the molecular weight of stabilizer resulted in a decrease in the molecular weight of the products.

One-pot aqueous phase synthesis of peptide–CdTe quantum dots

RSC Advances ◽  
2014 ◽  
Vol 4 (38) ◽  
pp. 20044-20047 ◽  
Author(s):  
Cuiling Zhang ◽  
Yuanyuan Zu ◽  
Xinghu Ji ◽  
Zhike He
Keyword(s):  
Quantum Dots ◽  
Aqueous Phase ◽  
High Salt ◽  
Cdte Quantum Dots ◽  
Salt Solutions ◽  
One Pot ◽  
Phase Synthesis ◽  
Short Peptide ◽  
Design And Synthesis ◽  
Excellent Stability

We report the design and synthesis of short peptide (hexapeptide)-capped CdTe quantum dots (peptide–QDs) by a one-pot method with excellent stability in acidic and high salt solutions.

scholarly journals Production and characterisation of a marine Halomonas surface-active exopolymer

2019 ◽  
Vol 104 (3) ◽  
pp. 1063-1076
Author(s):  
Tony Gutierrez ◽  
Gordon Morris ◽  
Dave Ellis ◽  
Barbara Mulloy ◽  
Michael D. Aitken
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Positive Influence ◽  
Contaminated Sites ◽  
Crude Oils ◽  
Magnetic Resonance Spectroscopic Analysis ◽  
Surface Active ◽  
Low Ionic Strength ◽  
Pure Hydrocarbon

AbstractDuring screening for novel emulsifiers and surfactants, a marine gammaproteobacterium, Halomonas sp. MCTG39a, was isolated and selected for its production of an extracellular emulsifying agent, P39a. This polymer was produced by the new isolate during growth in a modified Zobell’s 2216 medium amended with 1% glucose, and was extractable by cold ethanol precipitation. Chemical, chromatographic and nuclear magnetic resonance spectroscopic analysis confirmed P39a to be a high-molecular-weight (~ 261,000 g/mol) glycoprotein composed of carbohydrate (17.2%) and protein (36.4%). The polymer exhibited high emulsifying activities against a range of oil substrates that included straight-chain aliphatics, mono- and alkyl- aromatics and cycloparaffins. In general, higher emulsification values were measured under low (0.1 M PBS) compared to high (synthetic seawater) ionic strength conditions, indicating that low ionic strength is more favourable for emulsification by the P39a polymer. However, as observed with other bacterial emulsifying agents, the polymer emulsified some aromatic hydrocarbon species, as well as refined and crude oils, more effectively under high ionic strength conditions, which we posit could be due to steric adsorption to these substrates as may be conferred by the protein fraction of the polymer. Furthermore, the polymer effected a positive influence on the degradation of phenanthrene by other marine bacteria, such as the specialist PAH-degrader Polycyclovorans algicola. Collectively, based on the ability of this Halomonas high-molecular-weight glycoprotein to emulsify a range of pure hydrocarbon species, as well as refined and crude oils, it shows promise for the bioremediation of contaminated sites.

KINETIC EFFECTS OF HIGH MOLECULAR WEIGHT KININOGEN AND ZINC ON CONTACT ACTIVATION

1987 ◽  
Author(s):  
J D Shore ◽  
D E Day ◽  
S T Olson
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Proper Function ◽  
Factor Xii ◽  
High Molecular Weight Kininogen ◽  
Contact Activation ◽  
Kinetic Effects ◽  
Activation Rates ◽  
Kinetics Of

Previous work in our laboratory showed that Zn2+ enhanced the rate of kallikrein generation by dextran sulfate (DxSO4) in dialyzed normal plasma, but not in Fitzgerald or Hageman prismas. This could be partially explained by a marked effect of Zn2+ on factor XII autoactivation, and our present work involves zinc effects on other reactions of contact activation. At physiological ionic strength (0.15 μ), the kcat/Km for Xlla activation of prekallikrein (PK) was 0.62 μM™1 s™1 which was increased to 4.35 μM™1 s™1 by the presence of 25μg/ml DxSO4. High molecular weight kininogen (HMK) at 40 nM further increased this to 10.8 μM™1 s™1 , and 5 ¼M Zn2+ had no effect. To determine whether these cofactors promote a surface-dependent activation of PK by XIIa under conditions which weaken the protein-surface interactions, the kinetics were examined at 0.3μ. At this ionic strength, kcat/Km was 0.18 μM™1 s™1 and was unchanged by 25μg/ml DxSO4. This was increased to .805 μM™1 s™1 by 150 nM HMK and further increased 10-fold to 8.35 μM™1 s™1 by 10 μM™1 Zn2+ . Qualitative results were obtained at 0.3 μ for the other reciprocal reaction, XII activation by kallikrein (K). To observe XII activation within 2 hours, both 10 μM Zn2+ and 25 μM HMK were essential, indicating that these cofactors have a very large enhancing effect on the kinetics of this reaction. Chromatography of HMWK on DxSO4-agarose ^ljiowed elution of the protein at 0.42 M NaCl in the absence of Zn2+ ,but at 0.88M in its presence, providing evidence that Zn+ markedly increases the affinity of HMK for DxSO4. Our results are consistent with the increased activation rates observed in the presence of Zn2+ and HMK due to enhanced binding affinity of the reacting proteins to surfaces. This is likely to be essential for proper function of the contact system in blood, where many other proteins compete for surface. Supported by USPHS grant HL-25670

scholarly journals In-cloud processes of methacrolein under simulated conditions – Part 2: Formation of secondary organic aerosol

2009 ◽  
Vol 9 (14) ◽  
pp. 5107-5117 ◽  
Author(s):  
I. El Haddad ◽  
L. Nieto-Gligorovski ◽  
V. Michaud ◽  
B. Temime-Roussel ◽  
E. Quivet ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Aqueous Phase ◽  
Mass Concentration ◽  
Secondary Organic Aerosol ◽  
Organic Aerosol ◽  
Oh Radicals ◽  
Aerosol Formation ◽  
Esi Ms ◽  
Aerosol Mass Concentration

Abstract. The fate of methacrolein in cloud evapo-condensation cycles was experimentally investigated. To this end, aqueous-phase reactions of methacrolein with OH radicals were performed (as described in Liu et al., 2009), and the obtained solutions were then nebulized and dried into a mixing chamber. ESI-MS and ESI-MS/MS analyses of the aqueous phase composition denoted the formation of high molecular weight multifunctional products containing hydroxyl, carbonyl and carboxylic acid moieties. The time profiles of these products suggest that their formation can imply radical pathways. These high molecular weight organic products are certainly responsible for the formation of secondary organic aerosol (SOA) observed during the nebulization experiments. The size, number and mass concentration of these particles increased significantly with the reaction time: after 22 h of reaction, the aerosol mass concentration was about three orders of magnitude higher than the initial aerosol quantity. The evaluated SOA yield ranged from 2 to 12%. These yields were confirmed by another estimation method based on the hygroscopic and volatility properties of the obtained SOA measured and reported by Michaud et al. (2009). These results provide, for the first time to our knowledge, strong experimental evidence that cloud processes can act, through photooxidation reactions, as important contributors to secondary organic aerosol formation in the troposphere.

scholarly journals The polymerization of actin. III. Aggregates of nonfilamentous actin and its associated proteins: a storage form of actin.

1976 ◽  
Vol 69 (1) ◽  
pp. 73-89 ◽  
Author(s):  
L G Tilney
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Careful Examination ◽  
Filament Formation ◽  
Heavy Meromyosin ◽  
Associated Proteins ◽  
High Molecular Weight Proteins ◽  
Divalent Salts ◽  
Triton X

When echinoderm sperm are treated with the detergent Triton X-100 at pH 6.4 in 10 mM phosphate buffer, the membranes are solubilized, but the actin which is located in the periacrosomal region remains as a phase-dense cup. These cups can be isolated free from the flagella and chromatin and can be solubilized by increasing the pH to 8.0 and by changing the ionic strength and type of buffer used. Since the actin does not exist in the "F" state in unreacted sperm, and since the actin remains as a unit that does not diffuse away, it must be present in the mature sperm in a bound or storage state. The actin is, in fact, associated with a pair of proteins whose mol wt are 250,000 and 230,000. When the isolated cups are digested with trypsin, these high molecular weight proteins are digested, thereby liberating the actin. The actin will polymerize if heavy meromyosin or subfragment 1 is added to a preparation of isolated cups. Evidence is presented that this pair of high molecular weight proteins is similar in molecular weight and properties to erythrocyte spectrin. Attempts at transforming the storage form of actin in the cup into filaments were only moderately successful. The best conditions for filament formation involve incubating the cup in ATP and divalent salts. Careful examination of these cups reveals that the actin polymerized preferentially on either end of oriented filaments that already exist in the cup, indicating that self-nucleation is inefficacious. I conclude that the actin can exist in the storage form by its association with spectrin-like molecules and that the actin in this state polymerizes preferentially onto existing filaments.

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