The resemblance of the combination of human haptoglobin and double hemoglobin molecules to an antigen–antibody reaction

1970 ◽  
Vol 48 (2) ◽  
pp. 192-197 ◽  
Author(s):  
B. Malchy ◽  
G. H. Dixon
Keyword(s):  
Ionic Strength ◽  
Inbred Strain ◽  
Relative Concentration ◽  
Disc Electrophoresis ◽  
Precipitin Reaction ◽  
Antibody Reaction ◽  
Antigen Antibody ◽  
Low Ionic Strength

Human haptoglobin (Hp) combines with hemoglobin double molecules (Hb∙Hb) isolated from an inbred strain of mice, DBA/2J. When low ionic strength solutions of the two proteins are mixed, precipitates form. The extent of precipitation is dependent upon the ratios of the two proteins in a manner similar to that seen in a classical antigen–antibody precipitin reaction. In a more alkaline buffer of higher ionic strength, complexes form which remain soluble and may be resolved as a series of bands by acrylamide disc electrophoresis. The relative concentration of each band within the series depends upon the input ratios of Hp and Hb∙Hb. These results indicate that human haptoglobin is bivalent and combines with hemoglobin in a fashion analogous to the combination of an antibody with an antigen.

scholarly journals Effect of electrolytes and of distilled water on antigen–antibody complexes

1971 ◽  
Vol 125 (1) ◽  
pp. 297-302 ◽  
Author(s):  
Thérèse Ternynck ◽  
Stratis Avrameas
Keyword(s):  
Ionic Strength ◽  
Earth Metal ◽  
Electrolyte Solutions ◽  
Distilled Water ◽  
Metal Halides ◽  
Alkali Metal Halides ◽  
Solutions Of Electrolytes ◽  
Antigen Antibody ◽  
Low Ionic Strength ◽  
Free Antigen

Specific immune precipitates dissolve in concentrated solutions of alkali-metal halides, and of alkaline-earth-metal halides and thiocyanates. The quantity of protein dissolved depends on the nature of the antigen–antibody system, on the proportion of the antigen in the precipitate, and on the avidity of the antibody. The extent of solubilization is a function of the temperature, of the volume of solution used and of the concentration of the ions in the solution, and also depends on the nature of these ions. The dissolving power of bivalent cations is greater than that of monovalent ones, and is as follows: Mg2+[unk]Ba2+[unk]Ca2+[unk]Sr2+. Antigen–antibody complexes and free antibodies, but no free antigen, are detected in supernatants of specific precipitates dissolved in solutions of electrolytes of low ionic strength. Antigen–antibody complexes, free antibodies and also free antigen are detected in supernatants of specific precipitates dissolved in solutions of electrolytes of high ionic strength. Comparable results are obtained when the electrolyte solutions are studied for their effect on the bonds formed between an antibody and its corresponding immunosorbent. Moreover, in the latter case, 50% of the fixed antibodies could be recovered by elution with distilled water.

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

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).

An Evaluation of a Plasma Fractionation System

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.

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

1981 ◽  
Vol 193 (1) ◽  
pp. 375-378 ◽  
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.

scholarly journals Crystallization of tuna ferricytochrome c at low ionic strength.

1990 ◽  
Vol 265 (8) ◽  
pp. 4177-4180
Author(s):  
M H Walter ◽  
E M Westbrook ◽  
S Tykodi ◽  
A M Uhm ◽  
E Margoliash
Keyword(s):  
Ionic Strength ◽  
Ferricytochrome C ◽  
Low Ionic Strength

scholarly journals Reaction of Myosin with 1-Fluoro-2,4-dinitrobenzene at Low Ionic Strength

1969 ◽  
Vol 244 (3) ◽  
pp. 648-657 ◽  
Author(s):  
M Bárány ◽  
G Bailin ◽  
K Bárány
Keyword(s):  
Ionic Strength ◽  
Low Ionic Strength

scholarly journals Measuring pH in low ionic strength glacial meltwaters using ion selective field effect transistor (ISFET) technology

2021 ◽  
Author(s):  
Elizabeth A. Bagshaw ◽  
Jemma L. Wadham ◽  
Martyn Tranter ◽  
Alexander D. Beaton ◽  
Jon R. Hawkings ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Field Effect ◽  
Field Effect Transistor ◽  
Effect Transistor ◽  
Low Ionic Strength ◽  
Measuring Ph
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