scholarly journals Interaction Between Rabbit Erythroblast Ferritin and Normal Plasma Proteins

Blood ◽  
1974 ◽  
Vol 43 (6) ◽  
pp. 875-883 ◽  
Author(s):  
Hideo Yamada ◽  
Thomas G. Gabuzda ◽  
Marion Berenfeld
Keyword(s):  
Ionic Strength ◽  
Guinea Pig ◽  
Plasma Proteins ◽  
Starch Granule ◽  
Binding Activity ◽  
The Other ◽  
Heat Stable ◽  
Normal Plasma ◽  
Low Ionic Strength ◽  
Plasma Factors

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.

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 Chromatography of plasma proteins on immobilized Cibacron Blue F3-GA. Mechanism of the molecular interaction

1982 ◽  
Vol 203 (3) ◽  
pp. 637-641 ◽  
Author(s):  
E Gianazza ◽  
P Arnaud
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Molecular Interaction ◽  
Plasma Proteins ◽  
Hydrophobic Interactions ◽  
Molecular Characteristics ◽  
Acidic Ph ◽  
Cibacron Blue ◽  
Ligand Affinity ◽  
Low Ionic Strength

Fractionation of plasma proteins on immobilized Cibacron Blue F3-GA (Affi-gel Blue) under different conditions of pH, ionic strength and temperature was studied. At acidic pH the unbound proteins were eluted in order of increasing pI (the Affi-gel Blue behaving as ion-exchanger); at basic pH and at low ionic strength they were eluted in order of decreasing molecular weight (separation by diffusion-exclusion). For the proteins that were either retarded in comparison with substances of similar molecular characteristics, or that were bound to the resin, pseudo-ligand affinity or hydrophobic interactions were also implicated.

Binding of α2-macroglobulin and haptoglobin to Actinomyces pyogenes

1985 ◽  
Vol 31 (7) ◽  
pp. 657-659 ◽  
Author(s):  
Christoph Lämmler ◽  
Gursharan S. Chhatwal ◽  
Hans Blobel
Keyword(s):  
Immunoglobulin G ◽  
Steric Hindrance ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Binding Activity ◽  
The Other ◽  
Α2 Macroglobulin ◽  
Protein Nature ◽  
Actinomyces Pyogenes

All 25 cultures of Actinomyces pyogenes tested in the present study bound 125I-labelled human α2-macroglobulin with a mean binding of 65.6%. Thirteen cultures also bound 125I-labelled human haptoglobin with a mean of 51.5%. None interacted with fibrinogen, fibronectin, immunoglobulin G, or albumin. Twenty-eight cultures representing other species of actinomycetaceae did not show any interaction with α2-macroglobulin, haptoglobin, and other plasma proteins tested. The binding of α2-macroglobulin and haptoglobin to A. pyogenes was saturable and could be completely inhibited by the respective unlabelled plasma proteins. The binding of α2-macroglobulin could not be inhibited by unlabelled haptoglobin. On the other hand, α2-macroglóbulin blocked the binding of haptoglobin, possibly by steric hindrance. Treatment of the bacteria with trypsin reduced their binding activities for α2-macroglobulin and haptoglobin indicating the protein nature of the binding sites. Exposure to heat (1 h, 80 °C) significantly diminished the binding activity for haptoglobin, but not that for α2-macroglobulin. The binding of α2-macroglobulin and haptoglobin could be an important feature in the classification of A. pyogenes among the members of actinomycetaceae.

scholarly journals The Activation of Plasminogen by Hageman Factor and Hageman Factor Fragments

1977 ◽  
Author(s):  
G. Goldsmith ◽  
H. Saito ◽  
O.P. Ratnoff
Keyword(s):  
Ionic Strength ◽  
Kinetic Study ◽  
Mechanism Of Action ◽  
Amidolytic Activity ◽  
Direct Role ◽  
Hageman Factor ◽  
Normal Plasma ◽  
Low Ionic Strength

The mechanism of action of Hageman factor (HF, Factor Xll) in surface-mediated conversion of plasminogen to plasmin was investigated, assaying plasmin with H-D-valy 1-L-leucy1-L-1ysi ne p-nitroanalide·2HCL. Unexpectedly, amidolytic activity for this substrate evolved in the presence of kaolin in mixtures of purified preparations of plasminogen and HF, both devoid of detectable prekallikrein and high MW kininogen. The same result was obtained when plasminogen preparations were incubated in the absence of kaolin with HF-fragments prepared by digestion of HF with insoluble trypsin or with gel-filtered HF fragments (approximate MW 30,000). High MW kininogen did not enhance amidolysis in mixtures of plasminogen and HF with kaolin or HF fragments, but both amidolysis and fibrinolysis were enhanced by the fraction of normal plasma not absorbed at low ionic strength to QAE-Sephadex gels at ph 7-5-The analogous fraction of Fletcher trait (prekallikrein deficient) plasma, did not enhance amidolysis or fribrinolysi s. Kinetic study of the HF-kaolin-plasm inogen interaction indicated a direct enzymatic role for the HF moiety acting on plasminogen as a substrate.These data suggest that, contrary to earlier observations, HF or HF-fragments may play a direct role in the activation of plasminogen.

scholarly journals COMPONENTS OF GUINEA PIG COMPLEMENT

1963 ◽  
Vol 118 (5) ◽  
pp. 795-815 ◽  
Author(s):  
William D. Linscott ◽  
Kusuya Nishioka
Keyword(s):  
Guinea Pig ◽  
Deae Cellulose ◽  
Fluid Phase ◽  
Ammonium Hydroxide ◽  
Low Ph ◽  
The Other ◽  
Heat Stable ◽  
Heat Labile ◽  
High Degree ◽  
Pig Serum

The elution characteristics from DEAE cellulose are presented for four components of guinea pig serum, which are capable of interacting sequentially with sheep erythrocytes sensitized with antibody and the first, fourth, and second components of complement (EAC'1,4,2) to cause immune hemolysis, and information is given regarding some of the properties of these components, termed C'3c, C'3b, C'3a, and C'3d. All can react in the presence of ethylene-diaminetetraacetate, and are non-dialyzable. C'3c is quite stable at 56°C, but is rapidly inactivated at low pH or by contact with hydrazine or ammonium hydroxide. C'3b is moderately heat-stable, quite susceptible to low pH, and less readily destroyed by hydrazine. C'3a is very heat-labile, but relatively stable at low pH, while C'3d is heat-labile, sensitive to low pH, and insensitive to bydrazine. EAC'1,4,2 reacts with C'3c to form EAC'1,4,2,3c, which reacts then with C'3b to give the intermediate, EAC'1,4,2,3cb. The following reaction with C'3a yields EAC'1,4,2,3cba, which reacts finally with C'3d to give EAC'1,4, 2,3cbad (E*). The first and last reactions proceed moderately well at 0°C, but more rapidly at 30–37°C. The reaction with C'3b is almost completely inhibited at 0°C, while that involving C'3a proceeds almost as rapidly at 0°C as at higher temperatures. EAC'1,4,2,3cba cells have an increased fragility as compared with the other intermediate forms. Depletion studies with purified fractions and appropriate intermediate complexes showed a high degree of depletion of C'3c, somewhat less of C'3b, and little or no depletion of C'3a from the fluid phase. Examination of a beta1C globulin prepared from fresh human serum revealed high C'3c and C'3b activity, and very little C'3a or C'3d.

scholarly journals On Dielectric Constant and Enzymatic Kinetics

1962 ◽  
Vol 45 (4) ◽  
pp. 21-30 ◽  
Author(s):  
M. Castañeda-Agulló ◽  
Luz M. del Castillo
Keyword(s):  
Dielectric Constant ◽  
Ionic Strength ◽  
Linear Relationship ◽  
Salt Effect ◽  
The Other ◽  
Ion Structure ◽  
Glycine Solution ◽  
Enzymatic Kinetics ◽  
The One ◽  
Low Ionic Strength

A study was made on the effect of glycine on systems involving trypsin and BAEE1 or TSAME on the one hand, or α-chymotrypsin with any of the substrates BAEE, TEE, or PEE, on the other. In all cases there was a linear relationship between the rate logarithm and the reciprocal of the dielectric constant of the glycine solution. The slopes were positive in the reactions of trypsin. In those catalyzed by α-chymotrypsin, the slopes were positive at pH 6.5 or lower, and negative at pH 7.5. However, the effects of glycine differ quantitatively from those of urea or other solvents. The presence of salt modifies somewhat the glycine effects. A low ionic strength increases the effect of glycine on trypsin, but if the inhibition caused by the ionic strength is relatively strong, the addition of glycine partially neutralizes the salt effect. Addition of salt to systems containing α-chymotrypsin always resulted in a diminished effect of glycine. An attempt is made to interpret the anomalies of glycine effects on the basis of its dipolar ion structure.

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).

Comparative Study of Proactivators of the Fibrinolysin System in Three Mammalian Species

1969 ◽  
Vol 21 (03) ◽  
pp. 594-603 ◽  
Author(s):  
Y Takada ◽  
A Takada ◽  
J. L Ambrus
Keyword(s):  
Guinea Pig ◽  
Comparative Study ◽  
Human Plasma ◽  
Mammalian Species ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
The Other ◽  
Rabbit Plasma ◽  
Plate Test ◽  
Fibrin Plate

SummarySephadex gel filtration of human plasma gave results suggesting the presence of two proactivators of plasminogen, termed proactivators A and B.Activity resembling that of proactivator A was found in rabbit plasma, but not in guinea pig plasma.Plasminogen activators produced by the interaction of proactivator A of human plasma with streptokinase had no caseinolytic or TAMe esterolytic effect.Proactivator A can be separated in a form apparently free from plasminogen, as shown by the heated fibrin plate test and by immunological analysis. On the other hand, proactivator B concentrates prepared so far are contamined with plasminogen.Human proactivators appear to be far more susceptible to streptokinase than are rabbit proactivators.Inhibitors of the fibrinolysin system were observed in the plasmas of all 3 species. These inhibitors are not present in the euglobulin fraction of plasma. Sephadex fractionation of euglobulin fractions results in proactivator preparations that do not contain inhibitors.

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

1978 ◽  
Vol 88 (2) ◽  
pp. 298-305 ◽  
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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