Improved efficiency of mouse, guinea pig and human C3b inactivator at low ionic strength, and reproducible immune-adherence with mouse complement

Abstract Erythroblast ferritin (EF), isolated from phenylhydrazine-anemic rabbit marrow, interacts with components of normal plasma and forms a complex separable by starch granule electrophoresis and by dialysis techniques. The binding is facilitated at low ionic strength. The plasma factors responsible for binding EF are present in autologous, as well as homologous, plasma of normal nonimmune rabbits, although binding activities are quite variable in different plasmas. The binding activity for rabbit EF is also present in heterologous plasma of mouse, guinea pig, and man. The active principles in plasma were identified as two heat-stable components which fractionate as immunoglobulins, one as IgG and the other as IgM. The results support the hypothesis that natural antiferritin antibodies of low titer are present in normal plasma.

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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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An Evaluation of a Plasma Fractionation System

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654486 ◽

1960 ◽

Vol 4 (01) ◽

pp. 031-044

Author(s):

George Y. Shinowara ◽

E. Mary Ruth

Keyword(s):

Biological Activity ◽

Ionic Strength ◽

Plasma Proteins ◽

High Concentration ◽

Significant Evidence ◽

Native Proteins ◽

Mobility Data ◽

Fractionation Procedure ◽

The Individual ◽

Low Ionic Strength

SummaryFour primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S20, w and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S20, w classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

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THE RELATIVE DISTRIBUTION OF THYROXINE, TRIIODOTHYRONINE AND 3,3′,5′-(REVERSE)-TRIIODOTHYRONINE IN VARIOUS FRACTIONS OF THYROGLOBULIN

Acta Endocrinologica ◽

10.1530/acta.0.0880298 ◽

1978 ◽

Vol 88 (2) ◽

pp. 298-305 ◽

Cited By ~ 2

Author(s):

Peter Laurberg

Keyword(s):

Ionic Strength ◽

Guinea Pig ◽

Sucrose Gradient ◽

Deae Cellulose ◽

High Ionic Strength ◽

Relative Distribution ◽

Thyroid Extract ◽

Reverse Triiodothyronine ◽

Thyroid Secretion ◽

Stable Iodine

ABSTRACT Thyroglobulin fractions rich and poor in new thyroglobulin were separated by means of DEAE-cellulose chromatography of dog thyroid extracts and by zonal ultracentrifugation in a sucrose gradient of guinea pig thyroid extract incubated at low temperature. The distribution of thyroxine, triiodothyronine and 3,3′,5′-(reverse)-triiodothyronine in hydrolysates of the different fractions was estimated by radioimmunoassays. Following DEAE-cellulose chromatography there was a small but statistically significant increase in the T4/T3 ratio in thyroglobulin fractions eluted at high ionic strength - that is fractions relatively rich in stable iodine but poor in fresh thyroglobulin. There were no differences in the T4/rT3 ratios between the different fractions. The ratios between iodothyronines were almost identical in the various thyroglobulin fractions following zonal ultracentrifugation in a sucrose gradient of cold treated guinea pig thyroid extract. These findings lend no support to the possibility that a relatively high content of triiodothyronines in freshly synthesized thyroglobulin modulates the thyroid secretion towards a preferential secretion of triiodothyronine and 3,3′,5′-(reverse)-triiodothyronine at the expense of the secretion of thyroxine.

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Report on the U.S. Geological Survey's evaluation program for standard reference samples distributed in October 1993 : T-127 (trace constituents), M-128 (major constituents), N-40 (nutrients), N-41 (nutrients), P-21 (low ionic strength), Hg-17 (mercury), AMW-3 (acid mine water), and WW-1 (whole water)

Open-File Report ◽

10.3133/ofr9442 ◽

1994 ◽

Author(s):

H.K. Long ◽

J.W. Farrar

Keyword(s):

Ionic Strength ◽

Mine Water ◽

Acid Mine Water ◽

Evaluation Program ◽

Acid Mine ◽

Trace Constituents ◽

Low Ionic Strength ◽

Reference Samples ◽

The U.S ◽

Whole Water

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Results of the U.S. Geological Survey's Analytical Evaluation Program for standard reference samples: T-155 (trace constituents), M-148 (major constituents), N-59 (nutrient constituents), N-60 (nutrient constituents), P-31 (low ionic strength constituents), GWT-4 (ground-water trace constituents) and Hg-27 (Mercury) distributed in September 1998

Open-File Report ◽

10.3133/ofr9972 ◽

1999 ◽

Cited By ~ 1

Author(s):

Jerry W. Farrar

Keyword(s):

Ionic Strength ◽

Ground Water ◽

Analytical Evaluation ◽

Evaluation Program ◽

Trace Constituents ◽

Low Ionic Strength ◽

Reference Samples ◽

The U.S

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A novel procedure for the rapid purification of plastocyanin from pea (Pisum sativum) leaves

Biochemical Journal ◽

10.1042/bj1930375 ◽

1981 ◽

Vol 193 (1) ◽

pp. 375-378 ◽

Cited By ~ 4

Author(s):

A R Ashton ◽

L E Anderson

Keyword(s):

Ionic Strength ◽

Pisum Sativum ◽

Deae Cellulose ◽

High Concentrations ◽

Rapid Purification ◽

Low Ionic Strength

Plastocyanin is soluble at high concentrations (greater than 3 M) of (NH4)2SO4 but under these conditions will adsorb tightly to unsubstituted Sepharose beads. This observation was utilized to purify plastocyanin from pea (Pisum sativum) in two chromatographic steps. Sepharose-bound plastocyanin was eluted with low-ionic-strength buffer and subsequently purified to homogeneity by DEAE-cellulose chromatography.

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