Characterization of two Salmonella newport bacteriophages

1979 ◽  
Vol 25 (9) ◽  
pp. 1063-1072 ◽  
Author(s):  
N. Moazamie ◽  
H.-W. Ackermann ◽  
M. R. V. Murthy
Keyword(s):  
Molecular Weight ◽  
Melting Point ◽  
Acid Hydrolysis ◽  
Phage Particle ◽  
Size Classes ◽  
Salmonella Newport ◽  
Double Stranded Dna

Salmonella newport phages 16–19 and 7–11 have very long heads and are members of two rare and so far little-known phage groups. Both produce various morphological aberrations. Preparations of phage 7–11 contain numerous polyheads and about 0.4% short heads belonging to nine size classes. In addition, one giant phage particle was observed. The head of phage 7–11 seems to be an icosahedron which became elongated by adding successive rows of subunits. Phages 16–19 and 7–11 have buoyant densities in CsCl of 1.43 and 1.48 g/mL and particle weights of 103 and 204 × 106 respectively. Both viruses contain double-stranded DNA, internal proteins, and sugars. Phage 16–19 contains 46.5% DNA of 35 × 106 molecular weight, and glucose. Phage 7–11 contains 47.5% DNA of 108 × 106 molecular weight, and mannose. Base compositions of phage and S. newport DNAs were determined from buoyant densities, melting point, and acid hydrolysis. Phage 16–19 contains 5.4% 5-methylcytosine.

scholarly journals Synthesis of co-poly(eugenol sulfonate)-DVB from eugenol as a major component of Syzygium aromaticum oils

2004 ◽  
Vol 2 (2) ◽  
pp. 53-57 ◽  
Author(s):  
DESI SUCI HANDAYANI ◽  
TRIANA KUSUMANINGSIH ◽  
MARIA YULI
Keyword(s):  
Molecular Weight ◽  
Melting Point ◽  
Average Molecular Weight ◽  
Nitrogen Atmosphere ◽  
Capillary Viscometer ◽  
Syzygium Aromaticum ◽  
Number Average Molecular Weight ◽  
Solid Matter ◽  
Concentrated Sulfuric Acid

Cationic co-polymerization between eugenol and divinylbenzene (DVB) (2%, 4%, 6%, 8%, 10% and 12%) with BF3O(C2H5)2 as a catalyst at room temperature without media under nitrogen atmosphere has been investigated. Co-poly (eugenol sulfonate)-DVB has been synthesized by sulfonation of co-poly(eugenol-DVB). In the sulfonation, concentrated sulfuric acid was used as the reagent and Ag2SO4 as a catalyst. Structure and characterization of co-poly (eugenol-DVB) and Co-poly(eugenol sulfonate)-DVB were analyzed by Infra Red (IR), Differential Thermal Analysis) DTA and UV-Vis. Measurement of the number-average molecular weight (Mn) of copolymer was used Ostwald capillary viscometer. The yields of co-polymerization of eugenol-DVB were solid matter and the highest result was found on a copolymer of 10% of DVB. Its melting point was 69.33oC. The increasing of mole of DVB increase the number-average molecular weight (Mn) of co-poly (eugenol sulfonate)-DVB. A copolymer of 12% of DVB gave the highest molecular weight, Mn = 2984 g/mole. Synthesized of co-poly (eugenol sulfonate)- DVB were solid matter too and the highest result was found on a copolymer of 12% of DVB. Its melting point was 95.5oC.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

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.

Studies on the Characterization of Factor VIII and a Co-factor VIII

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
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
The Body ◽  
Haemophilia A ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Polysaccharide Content ◽  
Plasma Factor ◽  
Two Factors

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.

Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Gel Filtration ◽  
Chain Structure ◽  
The Other ◽  
Single Chain ◽  
Apparent Homogeneity ◽  
Sequential Adsorption

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.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

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.

Removal of Hydrophobic and Hydrophilic Constituents by Anion Exchange Resin

1999 ◽  
Vol 40 (9) ◽  
pp. 207-214 ◽  
Author(s):  
J.-P. Croué ◽  
D. Violleau ◽  
C. Bodaire ◽  
B. Legube
Keyword(s):  
Molecular Weight ◽  
Anion Exchange ◽  
Water Source ◽  
Atomic Ratio ◽  
Size Exclusion ◽  
Salting Out ◽  
Anion Exchange Resins ◽  
Hydrophilic Character ◽  
Exchange Resins

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.

Preparation and Characterization of the High Molecular Weight [3H]Hyaluronic Acid

1992 ◽  
Vol 57 (10) ◽  
pp. 2151-2156 ◽  
Author(s):  
Peter Chabreček ◽  
Ladislav Šoltés ◽  
Hynek Hradec ◽  
Jiří Filip ◽  
Eduard Orviský
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
High Molecular Weight ◽  
Methyl Bromide ◽  
High Performance ◽  
Hydrogen Atoms ◽  
Isolation And Characterization ◽  
Labelling Procedure ◽  
Enzymatic Depolymerization

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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