STUDIES ON FRANCIS INHIBITOR OF INFLUENZA VIRUS HAEMAGGLUTINATION IN RABBIT SERUM FRACTIONS OBTAINED BY ELECTROPHORESIS ON STARCH-GRAIN

2009 ◽  
Vol 44 (1) ◽  
pp. 92-105 ◽  
Author(s):  
Arild Harboe ◽  
Reidun Reenaas ◽  
Marit Oppedal
Keyword(s):  
Influenza Virus ◽  
Rabbit Serum ◽  
Serum Fractions ◽  
Starch Grain

scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1948 ◽  
Vol 87 (4) ◽  
pp. 315-328 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Type A ◽  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Virus Inhibitor ◽  
Virus Receptors

Evidence has been offered that influenza virus which has been heated at 56°C. for 30 or more minutes loses some of its capacity to agglutinate red cells and may completely lose its power to elute from cells on which it has been adsorbed. Such heat-inactivated virus does not possess the capacity to destroy the virus inhibitor in normal rabbit serum and this appears to be the explanation of the higher agglutinin inhibitory levels obtained with serum and heated virus as compared with serum and untreated virus. The heat-inactivated virus can be used to measure the inhibitor substance in normal rabbit serum. By two different methods it has been demonstrated that the inhibitor is destroyed in the presence of unheated influenza virus, as measured by inhibition titrations with virus inactivated at 56°C. The destruction of inhibitor by virus of either type A or B can be measured by virus of either type with similar results.

scholarly journals PURIFICATION OF AN INFLUENZA VIRUS SUBSTRATE, AND DEMONSTRATION OF ITS COMPETITIVE ANTAGONISM TO APPLE PECTIN

1949 ◽  
Vol 89 (1) ◽  
pp. 11-22 ◽  
Author(s):  
D. W. Woolley
Keyword(s):  
Influenza Virus ◽  
Calcium Ions ◽  
Water Soluble ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Apple Pectin ◽  
Alkaline Extract ◽  
Competitive Antagonism ◽  
Soluble Material

A substance was demonstrated in erythrocytes which antagonized the inhibiting effect of apple pectin on influenza virus hemagglutination. This substance was purified and found to be a water-soluble material, rather labile, and with some properties which suggested that it contained a polysaccharide. It was destroyed in vitro by highly purified preparations of the virus. It occurred in greatest amount in human erythrocytes and to a lesser extent in the red cells of species not susceptible to the virus. It was also found in normal rabbit serum. Calcium ions were found to be essential to the action of apple pectin in causing inhibition of virus hemagglutination. A second substance was purified from an alkaline extract of erythrocytes, and shown likewise to have an effect antagonistic to that of pectin. However, this latter material was not destroyed by the virus, and seemed to owe its effect to the binding of calcium ions.

Studies to assess the biological relevance of anti-Tamm–Horsfall protein antibodies detected by direct-binding enzyme-linked immunosorbent assay

1987 ◽  
Vol 73 (5) ◽  
pp. 479-487 ◽  
Author(s):  
J. S. Hunt ◽  
Anne Groufsky ◽  
K. L. Lynn
Keyword(s):  
Immunosorbent Assay ◽  
Guanidine Hydrochloride ◽  
Sodium Dodecyl ◽  
Rabbit Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serum Fractions ◽  
Direct Binding ◽  
Tract Infections ◽  
Sepharose 4B ◽  
Immune Rabbit

1. A role has been suggested for anti-Tamm–Horsfall protein (THP) antibodies in renal disease based on the results of immunoassays of pathological sera. The putative autoantibodies have not been isolated from such sera nor have definitive inhibition studies of their binding been carried out. We have carried out such studies using rabbit anti-THP antibodies as control reagents. 2. Urinary THP prepared by salt precipitation was used to prepare four immunoabsorbent columns by covalent coupling to CNBr-activated Sepharose 4B. After washing with a variety of dissociating agents to remove any non-covalently bound subunit THP, each column was incubated with normal and immune rabbit serum. Fractions washed and eluted from columns were tested for anti-THP antibodies by enzyme-linked immunosorbent assay (ELISA) and THP antigen by radioimmunoassay, and showed NH4SCN (3 mol/l) and guanidine hydrochloride (GuHCl) (6 mol/l) equivalent and sodium dodecyl sulphate (20 g/l) to be inferior in their capacity to produce immunoabsorbent THP capable of isolating specific antibodies from immune rabbit serum. 3. The column treated with GuHCl (6 mol/l) was used further in attempts to isolate putative anti-THP antibodies from five patients, who had a history of urinary tract infections and whose sera showed strong binding by ELISA. 4. Results from direct and inhibition ELISA experiments on fractions collected after washing and elution with all sera suggested that the putative human anti-THP antibodies were of very low affinity and/or directed against non-subunit THP. 5. The pathological relevance of human anti-THP antibodies measured by ELISA remains to be established.

scholarly journals ELECTROPHORETIC STUDY OF ANTIVIRAL SERA

1947 ◽  
Vol 85 (5) ◽  
pp. 515-530 ◽  
Author(s):  
Hilary Koprowski ◽  
Gilbert Richmond ◽  
Dan H. Moore
Keyword(s):  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Electrophoretic Study ◽  
Neutralizing Activity ◽  
Electrophoretic Patterns ◽  
Serum Fractions ◽  
Neutralizing Capacity ◽  
Before And After ◽  
Consistent Change ◽  
Γ Globulins

1. Sera of animals immunized against Japanese B encephalitis, Venezuelan equine encephalomyelitis, and Western equine encephalomyelitis viruses were fractionated by electrophoresis. 2. Electrophoretic patterns of rabbit sera before and after immunization against Japanese B virus showed no consistent change traceable to antibody formation. 3. To determine the antibody content, the electrophoretic fractions of the respective sera were mixed in varying dilutions with infected mouse brain suspensions, and the neutralizing titers of the fractions were compared. 4. In all instances serum fractions containing γ-globulin were protective, whereas in no case did serum albumin show any virus-neutralizing activity. The Japanese B encephalitis antibody appeared to be associated entirely with the γ-globulin. The Venezuelan and Western equine encephalomyelitis antibodies were associated with the ß- and γ-globulins and probably possessed an average electrophoretic mobility between that of ß- and γ-globulins. 5. Normal rabbit serum similarly separated electrophoretically showed no neutralizing properties. 6. Chickens, whose electrophoretic serum pattern is markedly different from that of rabbits, were also immunized against the Japanese B encephalitis virus. Their antisera were electrophoretically fractionated and similarly subjected to neutralization tests. The specific neutralizing capacity of chicken serum was considerably lower than that of rabbit serum and no neutralizing activity was found in the fractions containing the faster moving components. The antibody appeared to be associated with component 4 which had a mobility of approximately 2.3 x 10–5 cm.2/volt/sec.

scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1948 ◽  
Vol 87 (4) ◽  
pp. 301-314 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Sodium Periodate ◽  
Cell Receptor ◽  
Normal Serum ◽  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Red Cell ◽  
Virus Receptors ◽  
Serum Inhibitor

The influenza virus receptors of fowl red cells and the influenza virus inhibitor of normal rabbit serum have the following attributes in common: They are stable at high temperatures and in solutions of pH as high as 10.0. They both resist destruction by a number of oxidizing agents but are readily destroyed by sodium periodate, trypsin, and influenza virus. These facts suggest that the red cell receptor and the normal serum inhibitor are either the same or analogous substances and that they may belong to the mucoprotein class of compounds.

scholarly journals THE EFFECTS OF VARIOUS HORSE SERUM FRACTIONS IN PRODUCING CARDIOVASCULAR AND RENAL LESIONS IN RABBITS

1949 ◽  
Vol 90 (6) ◽  
pp. 577-594 ◽  
Author(s):  
Robert W. Wissler ◽  
Katharine Smull ◽  
James B. Lesh
Keyword(s):  
Sedimentation Rate ◽  
Heart Valves ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Pathological Findings ◽  
Serum Fractions ◽  
Before And After ◽  
Circulating Antigen ◽  
Acute Necrotizing ◽  
Tissue Sensitivity

Five groups of 10 rabbits each were injected intravenously 2 times at 15 day intervals with either whole horse serum or one of its cold alcohol-precipitated fractions. Suitable serological and general observations were made at appropriate intervals before and after each injection. All animals were sacrificed on the 22nd day of the experiment. A study of the antemortem and pathological findings led to the following conclusions. 1. Allergie arteritis, valvulitis, and to a lesser degree, focal pericarditis, Aschoff-like nodules, and glomerulitis can be produced by several of the cold alcohol-precipitated fractions of horse serum as well as by whole serum. 2. Most of the acute arteritis was seen in rabbits receiving fraction V (albumin). These rabbits showed the largest amounts of circulating antigen, low antibody titers, low tissue sensitivity, and slight elevation in sedimentation rate and temperature. 3. There was a high incidence of chronic arteritis in the rabbits receiving fraction III which is almost devoid of albumin, suggesting that the alpha and beta globulins in addition to albumin may produce arteritis. 4. A state most nearly resembling that of acute rheumatic fever was produced by either fractions III or IV-3,4 (alpha and beta globulins). Pancarditis (pericarditis, Aschoff-like lesions, and valvulitis) was found relatively frequently. Many of the rabbits developed a high sedimentation rate, elevated temperature, and high tissue sensitivity, but little acute arteritis was found in this group. 5. Gamma globulin (fraction II) produced little reaction either in the antemortem determinations or histopathologically. 6. Glomerulitis of an acute necrotizing type was seen in a few rabbits without particular correlation to the fraction injected. 7. The frequency of involvement of heart valves in rabbit serum disease follows a pattern very similar to that of rheumatic heart disesae. 8. Attempts to correlate antemortem observations and pathological findings either on a group basis or for individual animals failed.

63Ni Complexes in Rabbit Serum and Urine after Injection of 63NiCl2

1972 ◽  
Vol 18 (12) ◽  
pp. 1478-1484 ◽  
Author(s):  
Maria Van Soestbergen ◽  
F William Sunderman
Keyword(s):  
Renal Excretion ◽  
Physiological Role ◽  
Nickel Chloride ◽  
Rabbit Serum ◽  
Chromatographic Mobility ◽  
Serum Fractions ◽  
Nickel Homeostasis ◽  
Extracellular Transport ◽  
Serum And Urine

Abstract Radioactive nickel chloride (63NiCl2) was injected i.v. into rabbits in dosage of 0.24 mg Ni/kg body wt. 63Ni was rapidly cleared from the serum (T1/2 ≃ 8.2 h) during the period from 1 h to 2 days after the injection, but slowly (T1/2 ≃ 95 h) during the period from 4 to 7 days after the injection. During 24 h after injection of 63NiCl2, an average of 90% of serum 63Ni was bound to albumin and 10% was ultrafiltrable. Chromatography on Sephadex G-25 demonstrated the presence of five distinct 63Ni complexes (Fractions I to V) in serum ultrafiltrates. During 24 h after injection of 63NiCl2, an average of 78% of the administered dose of 63Ni was excreted in the urine. Chromatography of the urine on Sephadex G-25 separated three 63Ni complexes, which appeared to have identical chromatographic mobilities as serum Fractions II, III, and V. The chemical identities of the ultrafiltrable 63Ni complexes in serum and urine have not been established, although one (Fraction V) resembles Ni histidine in its chromatographic mobility on Sephadex G-25. This study demonstrates that ultrafiltrable nickel in serum and urine does not exist primarily as free Ni(II), but instead as Ni complexes, and suggests that ultrafiltrable Ni receptors play an important physiological role in nickel homeostasis by serving as diffusible vehicles for the extracellular transport and renal excretion of nickel.

Artifact-free electron microscopic immunocytochemistry on rat brain tissue

1991 ◽  
Vol 49 ◽  
pp. 272-273
Author(s):  
Veronika Burmeister ◽  
N. Ludvig ◽  
P.C. Jobe
Keyword(s):  
Microscopic Examination ◽  
Free Electron ◽  
Electron Microscopic Examination ◽  
Ultrastructural Localization ◽  
Rabbit Serum ◽  
Electron Microscopic ◽  
Electron Microscopic Immunocytochemistry ◽  
Phosphate Buffered Saline ◽  
Rat Brain Tissue ◽  
Immune Rabbit

Electron microscopic immunocytochemistry provides an important tool to determine the ultrastructural distribution of various molecules in both normal and pathologic tissues. However, the specific immunostaining may be obscured by artifactual immunoreaction product, misleading the investigator. Previous observations show that shortening the incubation period with the primary antibody from the generally used 12-24 hours to 1 hour substantially reduces the artifactual immunostaining. We now extend this finding by the demonstration of artifact-free ultrastructural localization of the Ca2/calmodulindependent cyclic nucleotide phosphodiesterase (CaM-dependent PDE) immunoreactivity in brain.Anesthetized rats were perfused transcardially with phosphate-buffered saline followed by a fixative containing paraformaldehyde (4%) and glutaraldehyde (0.25%) in PBS. The brains were removed, and 40μm sections were cut with a vibratome. The sections were processed for immunocytochemistry as described by Ludvig et al. Both non-immune rabbit serum and specific CaM-dependent PDE antibodies were used. In both experiments incubations were at one hour and overnight. The immunostained sections were processed for electron microscopic examination.

Detection of Viral Antigens in Mouse and Rat Tumor Cells by Immunoelectron Microscopy Following Periodate-Lysine-Paraformaldehyde (PLP) Fixation

1976 ◽  
Vol 34 ◽  
pp. 252-253
Author(s):  
Y. Ohtsuki ◽  
G. Seman ◽  
J. M. Bowen ◽  
M. Scanlon ◽  
L. Dmochowski
Keyword(s):  
Immunoelectron Microscopy ◽  
Mammary Tumor ◽  
Type A ◽  
Rabbit Serum ◽  
Virus Particles ◽  
Viral Antigens ◽  
Culture Cells ◽  
Mouse Mammary Tumor ◽  
Tumor Virus ◽  
Immunoperoxidase Labeling

Recently, periodate-lysine-paraformaldehyde (PLP) fixation was reported for immunoelectron microscopy (1). In PLP fixation, carbohydrates are oxidized by periodate and cross-linked by lysine; paraformaldehyde stabilizes proteins and lipids. By using PLP fixation, intracytoplasmic type A viral antigens have been previously demonstrated by immunoperoxidase labeling (2). In the present study, PLP fixation has been applied for the detection of the same antigens in mouse mammary tumor culture cells by both immunoferritin and immunoperoxidase methods. Rabbit anti-intracytoplasmic type A virus serum (anti-A), kindly provided by Dr. M. Muller (3), rabbit anti-strain A mouse mammary tumor virus (anti-MMTV) and preimmune rabbit serum as control were used to detect viral antigens in cells of C3H/HeJ strain mouse mammary tumor culture. Attempts have been also made to demonstrate peroxidase labeling of type C virus particles in frozen sections of an SD-MSV-induced NZB rat bone tumor tissue by rabbit anti-MuLV serum.

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