scholarly journals THE EMERGENCE OF ANTIBODIES WITH EITHER IDENTICAL OR UNRELATED INDIVIDUAL ANTIGENIC SPECIFICITY DURING REPEATED IMMUNIZATIONS WITH STREPTOCOCCAL VACCINES

1970 ◽  
Vol 131 (6) ◽  
pp. 1169-1189 ◽  
Author(s):  
Klaus Eichmann ◽  
Dietmar G. Braun ◽  
Ten Feizi ◽  
Richard M. Krause
Keyword(s):  
Electrophoretic Mobility ◽  
Specific Antibody ◽  
Carbohydrate Antigen ◽  
Unrelated Individual ◽  
Antigenic Specificity ◽  
Preparative Electrophoresis ◽  
Detectable Antibody ◽  
Electrophoretic Mobilities ◽  
Distinct Individual

Electrophoretically monodisperse antibody components in rabbit antisera to the carbohydrates of the Groups A and C streptococci have been examined for their individual antigenic specificity. In these antibody components which were isolated by preparative electrophoresis, individual antigenic specificity was confined to the specific antibody and was absent in the nonantibody γ-globulin. Radioprecipitation experiments and the use of immune absorbent columns constructed from goat anti-antisera, which had been absorbed with fraction II, revealed that all the specific antibody in an electrophoretically monodisperse component was reactive with the homologous anti-antibody. Antibodies with either identical or distinct individual antigenic specificities may occur in the same rabbit with repeated immunizations. Antibodies with identical antigenic specificity had identical electrophoretic mobility, whereas antibodies with unrelated antigenic specificities had distinct electrophoretic mobilities. In the interval between immunizations, if antibody to the carbohydrate antigen was absent, there was no detectable antibody with individual antigenic specificity.

scholarly journals Genetically determined polymorphism of the circulating human breast cancer-associated DF3 antigen

Blood ◽  
1988 ◽  
Vol 71 (2) ◽  
pp. 436-440 ◽  
Author(s):  
DF Hayes ◽  
H Sekine ◽  
D Marcus ◽  
CA Alper ◽  
DW Kufe
Keyword(s):  
Breast Cancer ◽  
Electrophoretic Mobility ◽  
Core Protein ◽  
Human Breast ◽  
Mobility Patterns ◽  
Multiple Alleles ◽  
Molecular Weights ◽  
The Core ◽  
Electrophoretic Mobilities ◽  
Genetically Determined

Abstract The murine monoclonal antibody (MAb) DF3 was prepared against a human breast carcinoma. Previous studies have demonstrated that DF3 antigen levels are elevated in plasma of patients with breast cancer. Furthermore, MAb DF3 reacts with circulating glycoproteins of different molecular weights ranging from approximately 300 to 450 kd. The present study demonstrates that plasma DF3 antigen is comprised of at least four moieties with slow (S), intermediate (I), rapid (R) and very rapid (VR) electrophoretic mobilities. The electrophoretic mobility patterns for circulating DF3 antigen differ among individuals. Moreover, DF3 antigen is detectable in urine, and the electrophoretic mobility of the urinary moieties is similar, but not identical, to that in the plasma. Studies in family members suggest that the electrophoretic heterogeneity of plasma DF3 antigen is determined by codominant expression of multiple alleles at a single locus. This locus may code for the core protein of DF3 antigen. These findings thus identify a genetically determined polymorphism of a circulating tumor-associated glycoprotein.

scholarly journals Comparison of mammalian mitochondrial ribosomal ribonucleic acid from different species

1972 ◽  
Vol 128 (5) ◽  
pp. 1033-1041 ◽  
Author(s):  
R. S. Mitra ◽  
B. Bartoov ◽  
J. Monahan ◽  
K. B. Freeman
Keyword(s):  
Ionic Strength ◽  
Electrophoretic Mobility ◽  
Density Gradients ◽  
Molecular Weights ◽  
Mitochondrial Rrna ◽  
Electrophoretic Mobilities ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Low Ionic Strength ◽  
Human And Mouse

Mitochondrial ribosomal RNA species from mouse L cells, rat liver, rat hepatoma, hamster BHK-21 cells and human KB cells were examined by electrophoresis on polyacrylamide–agarose gels and sedimentation in sucrose density gradients. The SE (electrophoretic mobility) and S values of mitochondrial rRNA of all species were highly dependent on temperature and ionic strength of the medium; the SE values increased and the S values decreased with an increase in temperature at a low ionic strength. At an ionic strength of 0.3 at 23–25°C or an ionic strength of 0.01 at 3–4°C the S and SE values were almost the same being about 16.2–18.0 and 12.3–13.6 for human and mouse mitochondrial rRNA. The molecular weights under these conditions were calculated to be 3.8×105–4.3×105 and 5.9×105–6.8×105, depending on the technique used. At 25°C in buffers of low ionic strength mouse mitochondrial rRNA species had a lower electrophoretic mobility than those of human and hamster. Under these conditions the smaller mitochondrial rRNA species of hamster had a lower electrophoretic mobility than that of human but the larger component had an identical mobility. Mouse and rat mitochondrial rRNA species had identical electrophoretic mobilities. Complex differences between human and mouse mitochondrial rRNA species were observed on sedimentation in sucrose density gradients under various conditions of temperature and ionic strength. Mouse L-cell mitochondrial rRNA was eluted after cytoplasmic rRNA on a column of methylated albumin–kieselguhr.

Δ Protein, a New Fibrous Protein of Skeletal Muscle: Preparation

1957 ◽  
Vol 188 (2) ◽  
pp. 205-211 ◽  
Author(s):  
William R. Amberson ◽  
John I. White ◽  
Howard B. Bensusan ◽  
Sylvia Himmelfarb ◽  
Brigitte E. Blankenhorn
Keyword(s):  
Skeletal Muscle ◽  
Ionic Strength ◽  
Electrophoretic Mobility ◽  
Protein A ◽  
High Ionic Strength ◽  
Partial Purification ◽  
Rabbit Muscle ◽  
Muscle Preparation ◽  
Preparative Electrophoresis ◽  
Fibrous Protein

Δ protein, a previously unreported fibrous protein with an electrophoretic mobility greater than that of myosin, is extracted from rabbit muscle by solutions of high ionic strength. This protein forms a complex with myosin, designated as Δ-myosin. Partial purification of Δ protein is achieved by two independent methods. In the first method alcohol fractionation is used. In the second, a solution of Salyrgan is used to dissociate the precipitated Δ-myosin complex. In each method further purification is obtained by preparative electrophoresis. Neither method yields a product which is entirely homogeneous. Tropomyosin is present as a contaminant in alcohol-fractionated preparations, and has been isolated and crystallized. All efforts to derive Δ protein from the previously known fibrous proteins of muscle have failed.

scholarly journals Conformational change in individual enzyme molecules

2015 ◽  
Vol 93 (6) ◽  
pp. 611-618 ◽  
Author(s):  
Jeremie J. Crawford ◽  
Frannie Itzkow ◽  
Joanna MacLean ◽  
Douglas B. Craig
Keyword(s):  
Heat Shock ◽  
Electrophoretic Mobility ◽  
Conformational Changes ◽  
Average Rate ◽  
Electrophoretic Mobilities ◽  
Significant Difference ◽  
Average Change ◽  
Before And After ◽  
Enzyme Molecules ◽  
Individual Enzyme

Single β-galactosidase molecule assays were performed using a capillary electrophoresis based protocol, employing post-column laser-induced fluorescence detection. In a first set of experiments, the distribution of single β-galactosidase molecule catalytic rates and electrophoretic mobilities were determined from lysates of Escherichia coli strains containing deletions for different heat shock proteins and grown under normal and heat shock conditions. There was no clear observed pattern of effect of heat shock protein expression on these distributions. In a second set of experiments, individual enzyme molecule catalytic rates were determined at 21 °C before and after 2 sequential brief periods of incubation at 50, 28, and 10 °C. The brief incubations at 50 °C caused a change in the enzyme molecules resulting in a different catalytic rate. Any given molecule was just as likely to show an increase in rate as a decrease, resulting in no significant difference in the average rate of the population. The average change in individual molecule rate was dependent upon the temperature of the brief incubation period, with a lesser average change occurring at 28 °C and negligible change at 10 °C. A third set of experiments was similar to that of the second with the exception that it was electrophoretic mobility that was considered. This provided a similar result. Incubation at higher temperature resulted in a change in electrophoretic mobility. The probability of an individual molecules switching to a higher mobility was approximately equal to that of switching to a lower mobility, resulting in no net average change in the population. The magnitude of the changes in electrophoretic mobilities suggest that the associated conformational changes are subtle.

Spherical-Shape Assumption for Protein–Aptamer Complexes Facilitates Prediction of their Electrophoretic Mobility

2019 ◽  
Author(s):  
Stanislav Beloborodov ◽  
Svetlana Krylova ◽  
Sergey Krylov
Keyword(s):  
Electrophoretic Mobility ◽  
Spherical Shape ◽  
Electrophoretic Mobilities ◽  
Source Data ◽  
Excel File

The pdf file describes the results of this study, which aims at developing a model to accurately predict electrophoretic mobilities of protein–aptamer complexes. The excel file contains source data for electropherograms (signal vs time) which were obtained in this study and used to determine the migration times and electrophoretic mobilities of proteins, aptamers, ssDNAs, protein–aptamer complexes, and protein–ssDNA complexes. Additional sheets in the excel file contain values of all migration times and mobilities obtained from the electropherograms.

Surface Modification and Electrophoresis of Normal and Transformed BHK21 Cells

1974 ◽  
Vol 14 (1) ◽  
pp. 203-214
Author(s):  
A. L. LATNER ◽  
G. A. TURNER
Keyword(s):  
Electrophoretic Mobility ◽  
Cell Types ◽  
Transformed Cells ◽  
Normal Cells ◽  
Neuraminidase Treatment ◽  
Total Histone ◽  
Electrophoretic Mobilities ◽  
Formaldehyde Treatment ◽  
The Mean ◽  
Number Of Cells

The mean electrophoretic mobilities at pH 7.5 of virus-transformed (Py6) and normal BHK21 cells were very similar, whether they were harvested mechanically or by the use of trypsin. After formaldehyde treatment, there was significantly increased mobility in both cell types; the transformed cells showed significantly the greater change. After neuraminidase treatment, the mean electrophoretic mobility was decreased to the same extent in both types of cell. Treatment with neuraminidase and formaldehyde had no effect on the mean electrophoretic mobility of the normal cells but slowed the transformed variety. The mobility in histone solution had no relationship to histone concentration but was statistically correlated with the amount of histone per cell, calculated from total histone present divided by the total number of cells; a linear relationship being obtained with the normal cells but an initial plateau was demonstrated with the transformed cells. The normal cell line showed a similar plateau after neuraminidase treatment. The possible significance of these results is discussed.

The Effecet Of Aspirin On The Activity Of Platelet Density Subpopulations As Measured By Electrophoretic Mobility

1981 ◽  
Author(s):  
R J LeBeau ◽  
J A Menna ◽  
R C Guntuer
Keyword(s):  
Electrophoretic Mobility ◽  
Electrophoretic Mobilities ◽  
Significant Difference ◽  
Male Subjects ◽  
Heavy Group ◽  
Light Medium

Whole populations of platelets were harvested from male subjects by centrifugation at 60g. Density subpopulations in the ranges: 1.040≤p1≤1.058, 1.058 ≤p2≤1.068, and 1.068 ≤p3≤1.080 were obtained using the Stractan method of Corash. These correspond approximately to the “light,” “medium,” and “heavy” subpopulations of Karpatkin. Electrophoretic mobilities (EB) of normal platelets and those following the subjects’ ingestion of aspirin where measured using a Zeiss Cytophero- meter. It is shown that there is a highly significant difference in EB between the three subpopulations of normal platelets and that the EB of the heavy group is significantly more affected by aspirin than that of the medium and light groups.

Serum Catalase: Reversibly Formed Charge Isoform of Erythrocyte Catalase

1991 ◽  
Vol 37 (12) ◽  
pp. 2043-2047 ◽  
Author(s):  
László Góth
Keyword(s):  
Electrophoretic Mobility ◽  
Serum Proteins ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Permeation Chromatography ◽  
Electrophoretic Mobilities ◽  
Erythrocyte Catalase ◽  
Gel Permeation ◽  
Human Sera ◽  
Molecular Masses

Abstract The different electrophoretic mobilities of erythrocyte and serum catalase (EC 1.11.1.6) were confirmed and the causes responsible for their differences were examined. The presence of a catalase-binding protein in serum that could form a complex with erythrocyte catalase was excluded by incubating serum proteins with erythrocyte catalase. No new unequivocal catalase bands representing a catalase-binding protein were detected. The erythrocyte and serum catalase proved to be charge isoforms: their molecular masses, estimated by gel permeation chromatography or polyacrylamide gel electrophoresis in a nondenaturing system, were very similar, whereas their electrophoretic mobilities were different. Assay of serum catalase by gel permeation and hydrophobic chromatography yielded a product with the same electrophoretic mobility as that of erythrocyte catalase. Different dilution of erythrocyte catalase with human sera led to a gradual decrease of its mobility, 20-fold or greater dilution yielding the same results as for serum catalase. Similarly, when serum catalase was diluted 20-fold or more with 60 mmol/L phosphate buffer, it migrated similarly to erythrocyte catalase. I detected no effect of dialyzable serum ligands, NADPH, or protection of SH groups on the electrophoretic mobility of either catalase isoform. I conclude that formation of charge isoforms of catalase is caused by a reversible, conformational modification due to matrix effect of serum.

Changes In Membrane Physicochemical Properties Of Hyperreactive Platelets In Estrogen-Treated Prostatic Cancer

1981 ◽  
Author(s):  
S M Jung ◽  
I Isohisa ◽  
K Kinoshita ◽  
H Yamazaki
Keyword(s):  
Sialic Acid ◽  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Prostatic Cancer ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostatic Hypertrophy ◽  
Factors Affecting ◽  
Glycoprotein I ◽  
Electrophoretic Mobilities

Aggregation and physicochemical properties of platelets from 5 prostatic cancer patients, 20 prostatic cancer on estrogen (300 mg stilbesterol diphosphate/day p.o.), 16 of the same patients given 300 mg aspirin/day, 19 prostatic hypertrophy and 21 aged males were examined. Prostatic cancer on estrogen show higher platelet aggregabilities towards ADP, adrenaline, and collagen than the other groups tested. Mean platelet electrophoretic mobilities were determined by the automatic Laser Zee 3000 system and the value for prostatic cancer on estrogen was -1.632±0.0182 um/sec/V/cm (mean ±SE). significantly higher (p <0.001)than the values for prostatic cancer not on estrogen, prostatic hypertrophy, and aged males with values of -1.534±0.0328, -1.526±0.009, and -1.535±0.012 um/sec/V/cm respectively. Electrophoretic mobility was a linear function of whole platelet sialic acid (r=0.96,n=66). The result suggests that the electrophoretic mobility of platelets was defined by sialic acid amount and there may be a selective consumption of platelets with less surface negative charge in prostatic cancer on estrogen. Membrane glycoprotein patterns determined by SDS-polyacrylamide gel electrophoresis showed prostatic cancer on estrogen to have lower glycoprotein I and higher glycoprotein IV than other groups (p < 0.05). There may be factors affecting changes on platelet membranes or population in such patients. Prostatic cancer on estrogen and aspirin had increased mobilities in 14 out of 16 cases with loss of linear relationship between mobility but no changes in sialic acid or glycoprotein pattern from those before aspirin. In vitro incubation of PRP with aspirin resulted in dose dependent increase in mobility with concomitant aggregability loss. The effect suggests another kind of inhibitory mechanism on platelet aggregation in addition to cyclooxygenase inhibition.

scholarly journals PAPAIN DIGESTION FRAGMENTS OF HUMAN IGM GLOBULINS

1968 ◽  
Vol 127 (3) ◽  
pp. 431-453 ◽  
Author(s):  
Constantin Mihaesco ◽  
Maxime Seligmann
Keyword(s):  
Electrophoretic Mobility ◽  
Degradation Process ◽  
Antigenic Specificity ◽  
High Yield ◽  
Small Peptides ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Early Stages ◽  
Carboxy Terminal ◽  
Papain Digestion

Papain digestion of two Waldenström IgM globulins produced a high amount of small peptides and resulted in the formation of two end products, the Fabµ and Fcµ fragments. The Fcµ fragment is characterized by a fast electrophoretic mobility, a high content in carbohydrate, and a high molecular weight. It was demonstrated that this fragment is made of heavy chain pieces belonging to several disulfide-linked monomeric subunits, presumably representing the carboxy-terminal end of the µ-chains. Fc fragments from the two macroglobulins could not be distinguished immunologically. An appreciable proportion of IgM molecules apparently underwent degradation without the formation of a stable Fc fragment. An Fc-like fragment, analogous to the reduced Fc fragment, was obtained at early stages of papain digestion of the IgM subunits. The Fabµ fragment, with slow and individually distinct electrophoretic mobility, bears many physicochemical and immunological similarities to the Fabγ fragment. It consists of one light chain and one Fd piece, both of which were isolated. The interaction of these two constituents was demonstrated by gel diffusion studies. Fab fragments of both IgM globulins were resolved into two subpopulations with different electric charges. In addition to these fragments, intermediary split products were observed at early stages of the degradation process, together with a high yield of small peptides mainly derived from the papain-sensitive region of the heavy chains. Immunologic data strongly suggested that this segment of µ-chains is situated between the Fd piece and the portion included in the Fc fragment. Several experiments indicated the importance of conformational antigenic specificity in both Fab and Fc regions of the IgM globulins.

Sign in / Sign up

Export Citation Format

Share Document