scholarly journals CHARACTERIZATION OF ALGINATE PREPARED FROM BROWN SEAWEEDS IN THUA THIEN-HUE PROVINCE, VIETNAM

2017 ◽  
Vol 25 (2) ◽  
pp. 427-433 ◽  
Author(s):  
Tran Vinh Thien ◽  
Chu Dinh Kinh ◽  
Tran Thai Hoa ◽  
Dinh Quang Khieu

The characterization of alginate prepared from brown seaweeds in TT-Hue province of Vietnam was investigated. Composition and the sequential structure of alginate were determined by 1HNMR, 13C-NMR, TOCSY, 1H-1H COSY, and 1H-13C-HSQC spectrum. It is found that alginate with molecular weight around 101 KDa is composed of homopolymeric regions of M and G blocks, interspersed with very small amount of regions of alternating structure of MG block.  This information is essential for application guideline of alginate in TT-Hue province.   

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.


1974 ◽  
Vol 31 (02) ◽  
pp. 328-338
Author(s):  
M. M. P Paulssen ◽  
H. L. M. A Vandenbussche-Scheffers ◽  
P. B Spaan ◽  
T de Jong ◽  
M. C Planje

SummaryFactor VIII occurs in the body in two different forms. In lymph factor VIII is bound to chylomicra. In plasma, factor VIII is bound to a protein.After delipidation of chylomicra we obtained a glycoprotein with a high polysaccharide content and a molecular weight of approx. 160,000.In plasma, factor VIII is attached to a protein which is present in normal concentrations in plasma of patients with haemophilia A and in serum (co-factor VIII).This factor is deficient in both the plasma and the serum of patients with von Willebrand’s disease.The binding between factor VIII and co-factor VIII is reversible.Some properties of these two factors are described.


1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.


1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.


2019 ◽  
Vol 9 (02) ◽  
Author(s):  
Zena G. Alrecabi ◽  
Zainab Amer ◽  
Naeemah Al-Lami

This study including prepared new colored esters containing heterocyclic with high molecular weights. In the first part of work we synthesized azo dyes [1,2] from the reaction p-toluidine with β-naphthol and o-nitro phenol, thin we synthesized Schiff bases [3,4] by the reaction anthranilic acid with benzaldehyde and dimethyl benzaldehyde. The reaction azo dyes (contain OH group) with Schiff base (contain COOH group) these led to produce the new colored esters [A1-A4]. The second part of work was modification the (C=N-) group in esters to heterocyclic compounds by reacting with phenyl iso cyanide to produce new β-lactam [B1-B4] and with anthranilic acid to get new hydroquinazoline [C1-C4]. All these compounds were characterized by physical properties and spectral methods FTIR, 1H-NMR and 13C-NMR.


2017 ◽  
Vol 68 (10) ◽  
pp. 2436-2439
Author(s):  
Stefania Felicia Barbuceanu ◽  
Laura Ileana Socea ◽  
Constantin Draghici ◽  
Elena Mihaela Pahontu ◽  
Theodora Venera Apostol ◽  
...  

In the work we presented the behavior of 5-(4-(4-X-phenylsulfonyl)phenyl)-4-(n-propyl)-2H-1,2,4-triazole-3(4H)-thiones (X= Cl or Br) with some alkylation agents. Thus, new S-alkylated 1,2,4-triazole derivatives were synthesized by reaction of the corresponding 1,2,4-triazole-3-thione derivatives with different �-halogenated compounds (ethyl bromide, ethyl chloroacetate or phenacyl bromide), in basic medium. The structures of synthesized compounds were elucidated by spectral data (1H-NMR, 13C-NMR, mass spectrometry) and elemental analysis.


1999 ◽  
Vol 40 (9) ◽  
pp. 207-214 ◽  
Author(s):  
J.-P. Croué ◽  
D. Violleau ◽  
C. Bodaire ◽  
B. Legube

The objective of this work was to compare the affinity of well characterized NOM fractions isolated from two surface waters with strong (gel matrix and macroporous matrix) and weak anion exchange resins (AER) using batch experiment conditions. The structural characterization of the fraction of NOM has shown that the higher the hydrophilic character, the lower the C/O atomic ratio, the lower the SUVA, the lower the aromatic carbon content and the lower the molecular weight. In general (not always), strong AER was more efficient to remove DOC than weak AER. For the same water source (Suwannee River), the higher the molecular weight of the NOM fraction, the lower the affinity with AER. Increasing the ionic strength favored the removal of the hydrophobic NOM fraction (“salting out” effect) while increasing the pH apparently reduced the removal of the hydrophilic NOM fraction. Results were discussed in terms of size exclusion, adsorption, anion exchange and also hydrophobic/hydrophilic repulsion.


1992 ◽  
Vol 57 (10) ◽  
pp. 2151-2156 ◽  
Author(s):  
Peter Chabreček ◽  
Ladislav Šoltés ◽  
Hynek Hradec ◽  
Jiří Filip ◽  
Eduard Orviský

Two methods for the preparation of high molecular weight [3H]hyaluronic acid were investigated. In the first one, hydrogen atoms in the molecule were replaced by tritium. This isotopic substitution was performed in aqueous solution using Pd/CaCO3 as the catalyst. In the second method, the high molecular weight hyaluronic acid was alkylated with [3H]methyl bromide in liquid ammonia at a temperature of -33.5 °C. High-performance gel permeation chromatographic separation method was used for the isolation and characterization of the high molecular weight [3H]hyaluronic acid. Molecular weight parameters for the labelled biopolymers were Mw = 128 kDa, Mw/Mn = 1.88 (first method) and Mw = 268 kDa, Mw/Mn = 1.55 (second method). The high molecular weight [3H]hyaluronic acid having Mw = 268 kDa was degraded further by specific hyaluronidase. Products of the enzymatic depolymerization were observed to be identical for both, labelled and cold biopolymer. This finding indicates that the described labelling procedure using [3H]methyl bromide does not induce any major structural rearrangements in the molecule.


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