Polysaccharides from the roots ofAlthaea officinalis L.: Structural features of D-glucans

1984 ◽  
Vol 49 (11) ◽  
pp. 2674-2679 ◽  
Author(s):  
Peter Capek ◽  
Rudolf Toman ◽  
Jozef Rosík ◽  
Alžbeta Kardošová ◽  
František Janeček
Keyword(s):  
Medicinal Plant ◽  
Structural Features ◽  
Gel Chromatography ◽  
Linear Character ◽  
Molecular Weights ◽  
Glycosidic Bonds ◽  
Althaea Officinalis ◽  
C Nmr

From the roots of the medicinal plant Althaea officinalis L., three D-glucans were isolated by gel chromatography which differed in molecular weights. The results of methylation analyses and 13C NMR measurements indicated predominantly linear character of the polysaccharide chains composed of α-D-glucopyranose units linked by 1 → 6 glycosidic bonds almost exclusively. The polymers had essentially the same structural features as D-glucan isolated from the leaves of this plant.

Glucan isolated from leaves of Althaea officinalis L.

1983 ◽  
Vol 48 (7) ◽  
pp. 2082-2087 ◽  
Author(s):  
Alžbeta Kardošová ◽  
Jozef Rosík ◽  
Rudolf Toman ◽  
Peter Capek
Keyword(s):  
Medicinal Plant ◽  
Periodate Oxidation ◽  
Linear Structure ◽  
Water Soluble ◽  
Partial Hydrolysis ◽  
Methylation Analysis ◽  
Glycosidic Bonds ◽  
Nmr Data ◽  
Althaea Officinalis ◽  
C Nmr

A water-soluble low-molecular D-glucan was isolated from leaves of the medicinal plant marsh-mallow (Althaea officinalis L.). The results of methylation analysis, partial hydrolysis, periodate oxidation, and 13C NMR data indicated a virtually linear structure with α-(1→6) glycosidic bonds.

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

Polysaccharides from the Flowers of Malva silvestris L., ssp. mauritiana (L.) THELL.: The Structure of D-Glucan

1992 ◽  
Vol 57 (11) ◽  
pp. 2400-2406 ◽  
Author(s):  
Peter Capek
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Average Molecular Weight ◽  
Linear Structure ◽  
Gel Chromatography ◽  
Spectroscopic Investigations ◽  
Glycosidic Bonds

The neutral polysaccharide α-D-glucan was isolated from the flowers of Malva silvestris L., ssp. mauritiana (L.) THELL. using a combination of ion exchange and gel chromatography. It was homogeneous under the conditions of free electrophoresis of average molecular weight Mn 25260. The chemical and spectroscopic investigations indicated a linear structure of the polysaccharide in which the α-D-glucopyranose units were linked predominantly by 1→6 glycosidic bonds, while some saccharides were the place of branching in position C-3.

scholarly journals The apparent molecular weights of human intestinal aminopeptidase, enterokinase and maltase in native duodenal fluid

1977 ◽  
Vol 165 (3) ◽  
pp. 583-585 ◽  
Author(s):  
A I Magee ◽  
D A W Grant ◽  
J Hermon-Taylor
Keyword(s):  
Molecular Form ◽  
Gel Chromatography ◽  
Duodenal Fluid ◽  
Molecular Weights ◽  
Induced Changes

The apparent molecular weights of human intestinal aminopeptidase, enterokinase and maltase in native duodenal fluid were estimated by gel chromatography on Sephadex G-200 under different conditions of operational buffer and temperature. No evidence for environmentally induced changes in molecular form was found.

THE EXTRACTION OF ORGANIC MATTER FROM SELECTED SOILS AND PARTICLE SIZE FRACTIONS WITH 0.5 M NaOH AND 0.1 M Na4P2O7 SOLUTIONS

1989 ◽  
Vol 69 (2) ◽  
pp. 253-262 ◽  
Author(s):  
M. SCHNITZER ◽  
P. SCHUPPLI
Keyword(s):  
Molecular Weight ◽  
Organic Matter ◽  
Humic Acids ◽  
Nmr Spectra ◽  
Attractive Alternative ◽  
Particle Size Fractions ◽  
Molecular Weights ◽  
Naoh Solution ◽  
C Nmr ◽  
Medium Silt

Organic matter (OM) in the Bainsville and Melfort soils, and in coarse clay and medium silt fractions separated from these soils, was extracted under N2 with 0.5 M NaOH and unadjusted 0.1 M Na4P2O7 solutions. pH ranges of the soils and fractions in contact for 24 h with 0.5 M NaOH and 0.1 M Na4P2O7 solutions extended from 12.2 to 12.6 and 9.0 to 9.4, respectively. Slightly greater proportions of the soil-carbon were extracted by 0.5 M NaOH than by 0.1 M Na4P2O7 solution. The differences, however, did not appear to be significant and may vary from soil to soil. The efficiency of extraction and the characteristics of the extracted materials were assessed on humic acids (HAs), which were isolated from the extracts. From the Bainsville soil and fractions, 0.1 M Na4P2O7 solution extracted more high-molecular weight and more deeply colored HAs than did 0.5 M NaOH solution. But HAs extracted from the Melfort soil and fractions had similar molecular weights and colours. 13C NMR spectra showed that HAs extracted by 0.1 M Na4P2O7 solution tended to be more aromatic than HAs extracted by 0.5 M NaOH solution. Well defined solid-state 13C NMR spectra of HAs, containing up to 69.0% ash, could be recorded. Unadjusted 0.1 M Na4P2O7 solution under N2 was found to be an attractive alternative to 0.5 M NaOH solution as an extractant for soil OM. Key words: Humic acids, E4:E6 ratios, IR spectra, 13C NMR spectra, aromaticity

Structure of Polybutadienes

1967 ◽  
Vol 40 (5) ◽  
pp. 1529-1543 ◽  
Author(s):  
W. S. Bahary ◽  
D. I. Sapper
Keyword(s):  
Light Scattering ◽  
Molecular Size ◽  
Structural Features ◽  
Melting Point Depression ◽  
Linear Polymers ◽  
Long Chain Branching ◽  
Molecular Weights ◽  
Catalyst Systems ◽  
Molecular Size Distribution

Abstract Polybutadienes made with six different catalyst systems were examined: (1) butyllithium, (2) “nickel-based”, (3) alfin, (4) “titanium-based”, (5) “cobalt-based”, and (6) free radical emulsion. The microstructure and macrostructure of the polybutadienes have been determined and are compared to the results published in the literature. These polybutadienes may be considered to be random terpolymers of cis, trans, and vinyl addition of butadiene. The glass transition temperature is specified by the vinyl content. The crystalline melting points of the high trans and also the high cis polybutadienes obey to a high measure Flory's equation for melting point depression of a random terpolymer. The molecular weights of the polybutadienes have been determined by light scattering and osmometry and the degree of long chain branching has been determined by the branching index, 〈g′〉. The macro-structural features of the linear polymers are confirmed by fractionation. However, the polydispersities calculated from fractionation data do not agree with those determined from light scattering and osmometry for the branched samples. The discrepancy is attributed to the method of characterization of the fractions. A distinction is made between molecular weight distribution and molecular size distribution.

Polymerization of n-butyl methylacrylate using bis(β- ketoamino)nickel(II)/MAO catalytic systems

e-Polymers ◽  
2008 ◽  
Vol 8 (1) ◽  
Author(s):  
Xiaohui He ◽  
Yiwang Chen ◽  
Yongming Liu ◽  
Muqing Chen ◽  
Shuxian Yu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monomer Concentration ◽  
Polymerization Temperature ◽  
Moderate Activity ◽  
Polymerization Time ◽  
Catalytic Systems ◽  
Molecular Weights ◽  
Molar Ratios ◽  
Broad Molecular Weight Distribution ◽  
C Nmr

AbstractThe polymerizations of n-butyl methylacrylate (nBMA) were carried out using bis(β-ketoamino)nickel(II) complexes (Ni[CH3C(O)CHC(NR)CH3]2: R = phenyl, 1; R = naphthyl, 2) in combination with methylaluminoxane (MAO) in toluene. The effect of parameters such as polymerization temperature, Al/Ni molar ratios, polymerization time, and monomer concentration, on catalytic polymerization activity and polymer molecular weights, were examined in detail. Both of the nickel(II) catalytic systems exhibited moderate activity, and produced P(nBMA) with high molecular weight and relatively broad molecular weight distribution (Mw/Mn=2.0~3.0. The obtained polymer has been characterized by means of FTIR, 1H NMR, 13C NMR, DSC, and WAXD technique and was confirmed to be syndio-rich stereospecific P(nBMA).

scholarly journals Partial purification and properties of the two common inherited forms of human erythrocyte adenylate kinase

1972 ◽  
Vol 130 (3) ◽  
pp. 797-803 ◽  
Author(s):  
C. Brownson ◽  
N. Spencer
Keyword(s):  
Adenylate Kinase ◽  
Effect Of Temperature ◽  
Partial Purification ◽  
Heat Denaturation ◽  
Gel Chromatography ◽  
Molecular Weights ◽  
Purification And Properties ◽  
Increasing Temperature

1. The partial purification of adenylate kinase, types 1 and 2, from human erythrocytes is described. 2. Gel chromatography of both forms of the enzyme gave estimates of the molecular weights in the range 20000–23000. 3. Studies on crude haemolysates at various pH values indicated that the type 2 enzyme was less stable than the type 1. Heat denaturation studies on the partially purified enzymes confirmed these findings. 4. Measurements of rates of inhibition by iodoacetate and iodoacetamide showed that the type 2 enzyme reacts more readily than the type 1 enzyme with both reagents. 5. The effect of temperature on the initial velocity of ADP formation was measured at a single concentration of both AMP and MgATP2-. The two forms of the enzyme responded differently to increasing temperature.

Studies on Soluble Fibrin Complexes as a Function of pH

1975 ◽  
Author(s):  
Y. Benabid ◽  
E. Concord ◽  
M. Suscillon
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Chromatography ◽  
Agarose Gel ◽  
Monomer Mixture ◽  
Soluble Fibrin ◽  
Molecular Weights ◽  
Fibrin Monomer

Purified fibrinogen solutions, incubated with thrombin. CNBr. Sepharose, were subjected to agarose gel chromatography and eluted at different pH (6.5; 7.5; 8.5). Among high molecular weight derivatives formed by thrombin, the major component was a dimer. Gel chromatography at pH 8.5 showed a complexes peak distinct of that from fibrinogen, whereas at pH 6.5, only the fibrinogen peak appeared: fibrin monomer was eluted with fibrinogen as demonstrated by polyacrylamid gel electrophoresis 3.75% pH 8.9. SDS urea electrophoresis after reduction indicated that complexes peak contained two α-chains (α and α′). When fibrinogen was incubated with thrombin in the presence of FSF and calcium, several derivatives with higher and higher molecular weights were formed besides the dimer, and elution profiles of chromatography were identical at pH 6.5 and 8.5, thus indicating stable complexes formation. If fibrinogen-fibrin monomer mixture was subjected to FSF action at different pH, no complexes were formed at pH 6.5. These results confirm that at pH 6.5, any association was prevented.

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