Thermodynamics of the interactions of sanguinarine with DNA: influence of ionic strength and base composition

Under a variety of electron microscope specimen preparation techniques different forms of chromatin appearance can be distinguished: beads-on-a-string, a 100 Å nucleofilament, a 250 Å fiber and a compact 300 to 500 Å fiber.Using a standardized specimen preparation technique we wanted to find out whether there is any relation between these different forms of chromatin or not. We show that with increasing ionic strength a chromatin fiber consisting of a row of nucleo- somes progressively folds up into a solenoid-like structure with a diameter of about 300 Å.For the preparation of chromatin for electron microscopy the avoidance of stretching artifacts during adsorption to the carbon supports is of utmost importance. The samples are fixed with 0.1% glutaraldehyde at 4°C for at least 12 hrs. The material was usually examined between 24 and 48 hrs after the onset of fixation.

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Conformational Transitions in Escherichia coli Ribosomal RNAs as Visualized by Dedicated STEM

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100102961 ◽

1988 ◽

Vol 46 ◽

pp. 176-177

Author(s):

J.S. Wall ◽

V. Maridiyan ◽

S. Tumminia ◽

J. Hairifeld ◽

M. Boublik

Keyword(s):

Ionic Strength ◽

Three Dimensional ◽

Conformational Transitions ◽

Dark Field ◽

Dimensional Structure ◽

Ribosomal Rnas ◽

Field Mode ◽

Freeze Dried ◽

High Resolution Images ◽

Low Ionic Strength

The high contrast in the dark-field mode of dedicated STEM, specimen deposition by the wet film technique and low radiation dose (1 e/Å2) at -160°C make it possible to obtain high resolution images of unstained freeze-dried macromolecules with minimal structural distortion. Since the image intensity is directly related to the local projected mass of the specimen it became feasible to determine the molecular mass and mass distribution within individual macromolecules and from these data to calculate the linear density (M/L) and the radii of gyration.2 This parameter (RQ), reflecting the three-dimensional structure of the macromolecular particles in solution, has been applied to monitor the conformational transitions in E. coli 16S and 23S ribosomal RNAs in solutions of various ionic strength.In spite of the differences in mass (550 kD and 1050 kD, respectively), both 16S and 23S RNA appear equally sensitive to changes in buffer conditions. In deionized water or conditions of extremely low ionic strength both appear as filamentous structures (Fig. la and 2a, respectively) possessing a major backbone with protruding branches which are more frequent and more complex in 23S RNA (Fig. 2a).

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Characterization of carbides in M50NiL

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100087343 ◽

1991 ◽

Vol 49 ◽

pp. 606-607

Author(s):

L. S. Lin ◽

K. P. Gumz ◽

A. V. Karg ◽

C. C. Law

Keyword(s):

Temperature Effects ◽

Base Composition ◽

Lattice Parameter ◽

Control Surface ◽

Carbide Formation ◽

Particle Sizes ◽

Low Carbon ◽

Fee Structure ◽

Heat Treated

Carbon and temperature effects on carbide formation in the carburized zone of M50NiL are of great importance because they can be used to control surface properties of bearings. A series of homogeneous alloys (with M50NiL as base composition) containing various levels of carbon in the range of 0.15% to 1.5% (in wt.%) and heat treated at temperatures between 650°C to 1100°C were selected for characterizations. Eleven samples were chosen for carbide characterization and chemical analysis and their identifications are listed in Table 1.Five different carbides consisting of M6C, M2C, M7C3 and M23C6 were found in all eleven samples examined as shown in Table 1. M6C carbides (with least carbon) were found to be the major carbide in low carbon alloys (<0.3% C) and their amounts decreased as the carbon content increased. In sample C (0.3% C), most particles (95%) encountered were M6C carbide with a particle sizes range between 0.05 to 0.25 um. The M6C carbide are enriched in both Mo and Fe and have a fee structure with lattice parameter a=1.105 nm (Figure 1).

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The three-dimensional structure of frozen-hydrated left- and right-handed forms of bacterial flagellar filaments from an identical serotype

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100143110 ◽

1986 ◽

Vol 44 ◽

pp. 298-299

Author(s):

S. Trachtenberg ◽

D. J. DeRosier

Keyword(s):

Ionic Strength ◽

Basal Body ◽

Three Dimensional ◽

Dimensional Structure ◽

Protein Species ◽

Liquid Environment ◽

Bacterial Flagellum ◽

Left And Right ◽

Rotary Motor ◽

Helical Parameters

The bacterial cell is propelled through the liquid environment by means of one or more rotating flagella. The bacterial flagellum is composed of a basal body (rotary motor), hook (universal coupler), and filament (propellor). The filament is a rigid helical assembly of only one protein species — flagellin. The filament can adopt different morphologies and change, reversibly, its helical parameters (pitch and hand) as a function of mechanical stress and chemical changes (pH, ionic strength) in the environment.

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Adsorption of chlorate and bromate ions on mercury electrodes from constant ionic strength solutions

Journal de Chimie Physique ◽

10.1051/jcp/1988850523 ◽

1988 ◽

Vol 85 ◽

pp. 523-527

Author(s):

M.M. Zuleika ◽

Palhares SILVA ◽

Ernesto Rafael GONZALEZ ◽

Luis Alberto AVACA ◽

Artur de Jesus MOTHEO

Keyword(s):

Ionic Strength ◽

Constant Ionic Strength ◽

Mercury Electrodes

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Antithrombin III Binding to Surface Immobilized Heparin and Its Relation to F Xa Inhibition

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646057 ◽

1987 ◽

Vol 58 (04) ◽

pp. 1064-1067 ◽

Cited By ~ 41

Author(s):

K Kodama ◽

B Pasche ◽

P Olsson ◽

J Swedenborg ◽

L Adolfsson ◽

...

Keyword(s):

Molecular Weight ◽

Ionic Strength ◽

Surface Coating ◽

Antithrombin Iii ◽

Lower Class ◽

Biologically Active ◽

High Affinity ◽

Heparin Coating ◽

Continuous Surface ◽

Approximate Molecular Weight

SummaryThe mode of F Xa inhibition was investigated on a thromboresistant surface with end-point attached partially depoly-merized heparin of an approximate molecular weight of 8000. Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT). The heparin surface adsorbed AT from both human plasma and solutions of purified AT. By increasing the ionic strength in the AT solution the existence of high and low affinity sites could be shown. The uptake of AT was measured and the density of available high and low affinity sites was found to be in the range of 5 HTid 11 pic.omoles/cmf, respectively Thus the estimated density of biologically active high and low ailmity heparm respectively would be 40 and 90 ng/cm2 The heparin coating did not take up or exert F Xa inhibition by itself. With AT adsorbed on both high and low affinity heparin the surface had the capacity to inhibit several consecutive aliquots of F Xa exposed to the surface. When mainly high affinity sites were saturated with AT the inhibition capacity was considerably lower. Tt was demonstrated that the density of AT on both high and low affinity heparin determines the F Xa inhibition capacity whereas the amount of AT on high affinity sites limits the rate of the reaction. This implies that during the inhibition of F Xa there is a continuous surface-diffusion of AT from sites of a lower class to the high affinity sites where the F Xa/AT complex is formed and leaves the surface. The ability of the immobilized heparin to catalyze inhibition of F Xa is likely to be an important component for the thromboresistant properties of a heparin coating with non-compromized AT binding sequences.

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Importance of Protease Inhibition in Studies on Purified Factor VIII (Antihaemophilic Factor)

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647943 ◽

1976 ◽

Vol 35 (01) ◽

pp. 186-190 ◽

Cited By ~ 6

Author(s):

Eugen A. Beck ◽

Peter Bachmann ◽

Peter Barbier ◽

Miha Furlan

Keyword(s):

Ionic Strength ◽

Factor Viii ◽

Gel Filtration ◽

High Ionic Strength ◽

Procoagulant Activity ◽

Carrier Protein ◽

Protease Inhibition ◽

Functional Sites ◽

Molecular Weight Peak ◽

Von Willebrand

SummaryAccording to some authors factor VIII procoagulant activity may be dissociable from carrier protein (MW~ 2 × 106) by agarose gel filtration, e.g. at high ionic strength. We were able to reproduce this phenomenon. However, addition of protease inhibitor (Trasylol) prevented the appearance of low molecular weight peak of factor VIII procoagulant activity both at high ionic strength and elevated temperature (37°C). We conclude from our results that procoagulant activity and carrier protein (von Willebrand factor, factor VIII antigen) are closely associated functional sites of native factor VIII macro molecule. Consequently, proteolytic degradation should be avoided in functional and structural studies on factor VIII and especially in preparing factor VIII concentrate for therapeutic use.

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