ULTRACENTRIFUGE AND DIFFUSION STUDIES ON GLUTEN

1942 ◽  
Vol 20c (3) ◽  
pp. 130-159 ◽  
Author(s):  
A. G. McCalla ◽  
Nils Gralén
Keyword(s):  
Sodium Salicylate ◽  
Minimum Weight ◽  
Average Molecular Weight ◽  
Sedimentation Equilibrium ◽  
Velocity Sedimentation ◽  
Molecular Characteristics ◽  
Weight Average Molecular Weight ◽  
Diffusion Constants ◽  
Diffusion Studies ◽  
And Diffusion

The molecular characteristics of gluten in sodium salicylate solutions were studied by means of sedimentation velocity, sedimentation equilibrium, and diffusion measurements. The proportion of total gluten protein molecularly dispersed increased with increase in concentration of sodium salicylate up to 12%, but the dispersed portions had essentially the same sedimentation constant (2.5 ± 0.15) regardless of the concentration of the dispersing medium.The most soluble 25 per cent of the gluten was all molecularly dispersed, but was definitely inhomogeneous. The weight-average molecular weight of this fraction was 44,000, but there is reason to believe the minimum weight may be about 35,000. None of the other fractions was entirely molecularly dispersed, the proportion decreasing with decreasing solubility of the fractions. Aggregates of many sizes existed in all of these fractions, but only the most insoluble contained aggregates large enough to cause opacity. Sedimentation constants of the molecularly dispersed portions increased slightly with decreasing solubility, while diffusion constants decreased markedly. None of the fractions yielded normal curves (diffusion diagrams) but the more soluble the fraction, the more nearly normal the curve. The inhomogeneity responsible for the varying rates of diffusion was due partly to differences in proportion and properties of the molecularly dispersed gluten and partly to aggregates.All properties showed progressive changes both within and between the arbitrarily produced fractions. These results, therefore, support the hypothesis that gluten is a protein system showing progressive and regular changes in properties with change in solubility.

scholarly journals The molecular weight of, and evidence for two types of subunits in, the molybdenum-iron protein of Azotobacter vinelandii nitrogenase

1977 ◽  
Vol 163 (3) ◽  
pp. 427-432 ◽  
Author(s):  
R H Swisher ◽  
M L Landt ◽  
F J Reithel
Keyword(s):  
Molecular Weight ◽  
Azotobacter Vinelandii ◽  
Average Molecular Weight ◽  
Amino Acid Content ◽  
Sedimentation Equilibrium ◽  
Weight Average Molecular Weight ◽  
Molybdenum Iron Protein ◽  
Iron Protein ◽  
Molecular Weights ◽  
Fe Protein

The weight-average molecular weight of the Mo-Fe protein isolated from Azotobacter vinelandii has been determined by sedimentation-equilibrium techniques. In buffer, the value is 245000+/-5000; in 8M-urea, the value is 61000+/-1000. The protein was separated into two components by chromatography on CM-cellulose in 7M-urea, pH 4.5. These components have similar molecular weights but were shown to differ in charge, amino acid content and arginine-containing peptides. It is proposed that the tetramer has the subunit composition (nalpha2nbeta2).

scholarly journals THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN

1935 ◽  
Vol 19 (1) ◽  
pp. 95-108 ◽  
Author(s):  
Michael Heidelberger ◽  
Kai O. Pedersen
Keyword(s):  
Molecular Weight ◽  
Isoelectric Point ◽  
Specific Volume ◽  
Sedimentation Equilibrium ◽  
Sedimentation Constant ◽  
Diffusion Constants ◽  
Equilibrium Data ◽  
Round Numbers ◽  
And Diffusion

1. The sedimentation constant of hog thyroglobulin is 19.2ċ10–13. That of human thyroglobulin is essentially the same. 2. The specific volume of hog thyroglobulin is 0.72. 3. The isoelectric point of native hog thyroglobulin is at pH 4.58, that of denatured thyroglobulin at pH 5.0. 4. The molecular weight of hog thyroglobulin is, in round numbers, 700,000, as calculated from the sedimentation and diffusion constants, or 650,000, as calculated from the sedimentation equilibrium data. 5. The thyroglobulin molecule deviates markedly from the spherical.

scholarly journals Molecular weight of Escherichia coli β-galactosidase in concentrated solutions of guanidine hydrochloride

1970 ◽  
Vol 120 (2) ◽  
pp. 255-261 ◽  
Author(s):  
Robert P. Erickson
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Guanidine Hydrochloride ◽  
Average Molecular Weight ◽  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Weight Average Molecular Weight ◽  
Random Coils ◽  
Equilibrium Sedimentation ◽  
Apparent Weight

The molecular weight of Escherichia coli β-galactosidase was determined in 6m- and 8m-guanidine hydrochloride by meniscus-depletion sedimentation equilibrium, sedimentation velocity and viscosity. Sedimentation equilibrium revealed heterogeneity with the smallest component having a molecular weight of about 50000. At lower speeds, the apparent weight-average molecular weight is about 80000. By use of a calculation based on an empirical correlation for proteins that are random coils in 6m-guanidine hydrochloride, sedimentation velocity gave a molecular weight of 91000, and the intrinsic viscosity indicated a viscosity-average molecular weight of 84000. Heating in 6m-guanidine hydrochloride lowered the viscosity of β-galactosidase in a variable manner.

Structure of the exudate gum from Meryta sinclairii

2020 ◽  
Author(s):  
Ian Sims ◽  
Richard Furneaux
Keyword(s):  
Average Molecular Weight ◽  
Gum Arabic ◽  
Arabinogalactan Protein ◽  
Weight Average Molecular Weight ◽  
1H And 13C Nmr ◽  
One Dimensional ◽  
Linkage Analyses ◽  
Yariv Reagent ◽  
Native Tree ◽  
High Level

A gum that exudes from the wounded trunk of the New Zealand native tree Meryta sinclairii has been isolated. The gum was completely precipitated by the β-glucosyl Yariv reagent and was thus determined to be an arabinogalactan-protein (AGP). It contained >95% w/w carbohydrate and only 2% w/w protein with a high level of hydroxyproline. SEC-MALLS showed that the gum had a weight-average molecular weight of 4.45×106Da compared with 6.02×105Da for gum arabic. Constituent sugar and linkage analyses were consistent with polymers comprised of a highly branched backbone of 1,3-linked galactopyranosyl (Galp) residues, with side-chains made up of arabinofuranose- (Araf) containing oligosaccharides, terminated variously by rhamnopyranosyl (Rhap), arabinopyranosyl (Arap), Galp and glucuronopyranosyl (GlcpA) residues. Analysis by one-dimensional and two-dimensional 1H and 13C NMR experiments confirmed the linkage analyses. The structure of the gum is discussed in comparison with the structure of gum arabic and other AGPs. © 2003 Elsevier Science Ltd. All rights reserved.

Molecular, rheological and physicochemical characterisation of puka gum, an arabinogalactan-protein extracted from the Meryta sinclairii tree

2020 ◽  
Author(s):  
MSM Wee ◽  
Ian Sims ◽  
KKT Goh ◽  
L Matia-Merino
Keyword(s):  
Hydrodynamic Radius ◽  
Average Molecular Weight ◽  
Gum Arabic ◽  
Water Soluble ◽  
Arabinogalactan Protein ◽  
Type Ii ◽  
Weight Average Molecular Weight ◽  
Soluble Polysaccharide ◽  
Physicochemical Characterisation ◽  
Increasing Temperature

© 2019 Elsevier Ltd A water-soluble polysaccharide (type II arabinogalactan-protein) extracted from the gum exudate of the native New Zealand puka tree (Meryta sinclairii), was characterised for its molecular, rheological and physicochemical properties. In 0.1 M NaCl, the weight average molecular weight (Mw) of puka gum is 5.9 × 106 Da with an RMS radius of 56 nm and z-average hydrodynamic radius of 79 nm. The intrinsic viscosity of the polysaccharide is 57 ml/g with a coil overlap concentration 15% w/w. Together, the shape factor, p, of 0.70 (exponent of RMS radius vs. hydrodynamic radius), Smidsrød-Haug's stiffness parameter B of 0.031 and Mark-Houwink exponent α of 0.375 indicate that the polysaccharide adopts a spherical conformation in solution, similar to gum arabic. The pKa is 1.8. The polysaccharide exhibits a Newtonian to shear-thinning behaviour from 0.2 to 25% w/w. Viscosity of the polysaccharide (1 s−1) decreases with decreasing concentration, increasing temperature, ionic strength, and at acidic pH.

Metathesis Polymerization of Phenylacetylene by Tungsten Aryloxo Complexes

1995 ◽  
Vol 60 (3) ◽  
pp. 489-497 ◽  
Author(s):  
Hynek Balcar ◽  
Jan Sedláček ◽  
Marta Pacovská ◽  
Vratislav Blechta
Keyword(s):  
Molecular Weight ◽  
Catalytic Activity ◽  
Induction Period ◽  
Average Molecular Weight ◽  
Molar Fraction ◽  
Molar Ratio ◽  
Weight Average Molecular Weight ◽  
Polymer Yield ◽  
Positive Effect ◽  
Ligand Addition

Catalytic activity of the tungsten aryloxo complexes WCl5(OAr) and WOCl3(OAr), where Ar = 4-t-C4H9C6H4, 2,6-(t-C4H9)2C6H3, 2,6-Cl2C6H3, 2,4,6-Cl3C6H2, and 2,4,6-Br3C6H2 in polymerization of phenylacetylene (20 °C, monomer to catalyst molar ratio = 1 000) was studied. The activity of WCl5(OAr) as unicomponent catalysts increases with increasing electron withdrawing character of the -OAr ligand. Addition of two equivalents of organotin cocatalysts (Me4Sn, Bu4Sn, Ph4Sn, Bu3SnH) to WCl5(O-C6H2Cl3-2,4 ,6) has only slight positive effect (slightly higher polymer yield and/or molecular weight of poly(phenylacetylene)s was achieved). However, in the case of WOCl3(O-C6H3Cl2-2, 6) catalyst, it enhances the activity considerably by eliminating the induction period. Poly(phenylacetylene)s prepared with the catalysts studied have weight-average molecular weight ranging from 100 000 to 200 000. They are trans-prevailing and have relatively low molar fraction of monomer units comprised in cyclohexadiene sequences (about 6%).

Gold implantation inn‐type silicon: Entropy factor and diffusion studies

1990 ◽  
Vol 68 (4) ◽  
pp. 1601-1605 ◽  
Author(s):  
S. Coffa ◽  
L. Calcagno ◽  
G. Ferla ◽  
S. U. Campisano
Keyword(s):  
Type Silicon ◽  
Diffusion Studies ◽  
Entropy Factor ◽  
And Diffusion

Pollution plume transport and diffusion studies using fluorescence lidar

1980 ◽  
Vol 19 (15) ◽  
pp. 2524 ◽  
Author(s):  
Burton G. Schuster ◽  
Thomas G. Kyle
Keyword(s):  
Diffusion Studies ◽  
Transport And Diffusion ◽  
Plume Transport ◽  
And Diffusion

Sorption and diffusion studies in cementitious grouts

1992 ◽  
Vol 12 (2-3) ◽  
pp. 289-297 ◽  
Author(s):  
H.M. Johnston ◽  
D.J. Wilmot
Keyword(s):  
Diffusion Studies ◽  
And Diffusion
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