scholarly journals INFLUENCE OF EXTRANEOUS PROTEIN AND VIRUS CONCENTRATION ON THE INACTIVATION OF THE RABBIT PAPILLOMA VIRUS BY X-RAYS

1941 ◽  
Vol 74 (5) ◽  
pp. 463-487 ◽  
Author(s):  
William F. Friedewald ◽  
Rubert S. Anderson
Keyword(s):  
Rabbit Serum ◽  
Virus Concentration ◽  
Normal Rabbit Serum ◽  
X Rays ◽  
Papilloma Virus ◽  
Egg Albumin ◽  
Buffer Solutions ◽  
Dilute Suspensions ◽  
Antiviral Antibody ◽  
Extraneous Material

The pronounced resistance to the x-rays manifested by the papilloma virus in ordinary suspensions is due to the protecting influence of extraneous matter and also in considerable degree to the amount of virus present in the preparation. Two to 4 million r were required to inactivate the virus contained in the crude papilloma extracts prepared for the present work, whereas 100,000 r or less was enough to inactivate comparable concentrations of virus after extraneous matter had been excluded by repeated differential centrifugation. The addition of normal rabbit serum or crystalline egg albumin to purified suspensions of virus was found to increase greatly the amount of irradiation required to inactivate the virus. Furthermore the percentage destruction of virus by a given amount of irradiation increases as the concentration is decreased by dilution with saline or buffer solutions. As little as 3,000 r will inactivate much of the virus in very dilute suspensions. The complement-binding antigen of papilloma virus suspensions is also inactivated by x-rays, but requires a somewhat larger amount of irradiation than necessary to destroy the infectivity of the suspensions. The effects of irradiation on the antiviral antibody present in the blood of animals which have become immune to the virus—an antibody that specifically fixes complement in mixture with the papilloma virus—are also conditioned by extraneous material. 250,000 to 500,000 r had only a slight effect on the antibody in whole serum, while this amount of irradiation completely inactivated comparable amounts of antibody in preparations partially purified by precipitation with ammonium sulfate. As a whole the findings indicate that under certain conditions of purity and concentration most of the radiation does not act by direct hits on virus or antibody particles, but indirectly by ionizing or exciting some other molecules present in the exposed suspension, which then react with the virus or antibody molecules.

scholarly journals THE EFFECT OF SALICYLATES ON THE PRECIPITATION OF ANTIGEN WITH ANTIBODY

1943 ◽  
Vol 77 (2) ◽  
pp. 173-183 ◽  
Author(s):  
Alvin F. Coburn ◽  
Eleanor M. Kapp
Keyword(s):  
Immune System ◽  
Sodium Salicylate ◽  
Sodium Tungstate ◽  
Horse Serum ◽  
Rabbit Antiserum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Egg Albumin ◽  
Immune Precipitation ◽  
Lyotropic Series

1. Sodium salicylate modifies the precipitation of normal rabbit serum protein by sodium tungstate, and partially inhibits the precipitation of horse serum euglobulin by rabbit antiserum. Sodium salicylate added to a system containing crystalline egg albumin and its antibody partly prevents the formation of precipitate, the degree of inhibition being related to the concentration of salicylate. 2. Precipitation in the equivalence zone is more readily prevented by salicylate than precipitation in the region of antibody excess, the immune system becoming progressively less sensitive to the action of salicylate as the excess of antibody becomes larger. 3. Formed precipitates were partly dissolved following resuspension in the presence of salicylate. 4. The salicylate effect on immune precipitation is reversible, and appears to be due to inactivation of antibody. 5. Salicylate was more effective in preventing specific precipitation than other anions of a lyotropic series tested.

scholarly journals ELECTROPHORETIC STUDIES ON ELEMENTARY BODIES OF VACCINIA

1940 ◽  
Vol 72 (5) ◽  
pp. 511-521 ◽  
Author(s):  
Theodore Shedlovsky ◽  
Joseph E. Smadel
Keyword(s):  
Moving Boundary ◽  
Serum Proteins ◽  
Vaccine Virus ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Buffer Solution ◽  
Buffer Solutions ◽  
Heat Stable ◽  
Heat Stable Antigen ◽  
Sufficient Magnitude

Electrophoretic studies were made on vaccine virus, collodion particles, and glass particles suspended in 0.01 molar buffer solutions at pH 7.9, in which the moving boundary method was used. In some experiments, uncoated particles were used; in others, particles were coated with proteins and then resuspended in the buffer solution after a washing; in still others, an excess of protein which had been used to coat the particles was included in the buffer medium. Streaming boundaries were obtained with all dilute suspensions of particles in solutions containing no soluble protein instead of the flat ones usually observed with the Tiselius moving boundary technique. This boundary artifact was suppressed by maintaining a density gradient of sufficient magnitude in association with the moving boundary to counteract the tendency of endosmotic flow. This was done partially by increasing the concentration of the particles in the suspensions, and almost completely by retaining an excess of soluble-coating substance in the solutions containing the particles. The mobility of elementary bodies of vaccinia corresponds to that found for the heat-stable (S) antigen. This value was not altered by drying, heating, ether extraction, or simple washing, but was materially increased by treatment with the surface active detergent (duponol) which presumably altered the nature of the surface of the virus particles. Collodion particles coated with the heat-stable antigen of vaccinia had the same mobility as elementary bodies under comparable conditions. Glass particles coated with normal rabbit serum moved at the rate of albumin, the fastest serum component in the buffer solutions used. However, both collodion particles and vaccine virus moved at a somewhat slower rate when they were similarly coated and measured in the presence of an excess of serum in the solutions. This was probably due to adsorption of a small amount of one of the slower components (globulin) of rabbit serum on the surface of the particles. Simple washing after treatment seemed to remove the coating of serum proteins, at least in part, from both collodion particles and elementary bodies of vaccinia.

Identification of Maize Rayado Fino Virus by Immunoelectron Microscopy

1985 ◽  
Vol 43 ◽  
pp. 636-637
Author(s):  
O. E. Bradfute
Keyword(s):  
Electron Microscopy ◽  
Zea Mays ◽  
Costa Rica ◽  
Severe Disease ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Virus Particles ◽  
Far North ◽  
Maize Rayado Fino Virus ◽  
Antibody Coating

Maize rayado fino virus (MRFV) causes a severe disease of corn (Zea mays) in many locations throughout the neotropics and as far north as southern U.S. MRFV particles detected by direct electron microscopy of negatively stained sap from infected leaves are not necessarily distinguishable from many other small isometric viruses infecting plants (Fig. 1).Immunosorbent trapping of virus particles on antibody-coated grids and the antibody coating or decoration of trapped virus particles, was used to confirm the identification of MRFV. Antiserum to MRFV was supplied by R. Gamez (Centro de Investigacion en Biologia Celular y Molecular, Universidad de Costa Rica, Ciudad Universitaria, Costa Rica).Virus particles, appearing as a continuous lawn, were trapped on grids coated with MRFV antiserum (Fig. 2-4). In contrast, virus particles were infrequently found on grids not exposed to antiserum or grids coated with normal rabbit serum (similar to Fig. 1). In Fig. 3, the appearance of the virus particles (isometric morphology, 30 nm diameter, stain penetration of some particles, and morphological subunits in other particles) is characteristic of negatively stained MRFV particles. Decoration or coating of these particles with MRFV antiserum confirms their identification as MRFV (Fig. 4).

Localization of oxytocin and neurophysin in baboon (Papio anubis) corpus luteum by immunocytochemistry

1986 ◽  
Vol 113 (4) ◽  
pp. 570-575 ◽  
Author(s):  
Firyal S. Khan-Dawood
Keyword(s):  
Corpus Luteum ◽  
Rabbit Serum ◽  
Corpora Lutea ◽  
Positive Staining ◽  
Normal Rabbit Serum ◽  
Fallopian Tubes ◽  
Papio Anubis ◽  
Luteal Cells ◽  
Luteal Tissue ◽  
Immunocytochemical Reaction

Abstract. Immunoreactive oxytocin is detectable in the corpora lutea of women and cynomolgus monkeys by radioimmunoassay. To localize the presence of oxytocin and neurophysin I in ovarian tissues of subhuman primates, three corpora lutea and ovarian stromal tissues and two Fallopian tubes obtained during the menstrual cycle of the baboon and decidua from two pregnant baboons were examined using highly specific antisera against either oxytocin or neurophysin I and preoxidase-antiperoxidase light microscopy immunohistochemistry. Oxytocin-like as well as neurophysin I-like immunoreactivities were found in some cells of all the corpora lutea only, but could not be demonstrated in ovarian stromal tissues, Fallopian tubes and decidua. Specificity of the immunocytochemical reaction was further confirmed by immunoabsorption of the antiserum with excess oxytocin or neurophysin, after which the immunoreactivities for both oxytocin and neurophysin in the luteal tissue were negative. Similar controls using normal rabbit serum gave no positive staining for either oxytocin or neurophysin. Counterstaining of the positive immunoreactivities for oxytocin and neurophysin I with Mayer's haematoxylin and eosin demonstrated clearly that the oxytocin and neurophysin I appeared as granular material mainly within the cytoplasm of the luteal cells. The localization of immunoreactive oxytocin and neurophysin I in the corpus luteum of the baboon demonstrates directly the presence of these two neurohypophysial peptides within primate luteal cells and suggests their local production.

scholarly journals THE EFFECTS OF ROENTGEN RAYS ON CELL-VIRUS ASSOCIATIONS

1943 ◽  
Vol 78 (4) ◽  
pp. 285-304 ◽  
Author(s):  
William F. Friedewald ◽  
Rubert S. Anderson
Keyword(s):  
X Rays ◽  
Pathological Changes ◽  
Cellular Division ◽  
Papilloma Virus ◽  
X Ray ◽  
Crude Extracts ◽  
Domestic Rabbits ◽  
Roentgen Rays

The virus-induced papillomas of cottontail as well as domestic rabbits regress completely within a few weeks when exposed to 5,000 r of x-ray irradiation. The x-rays do not immediately kill the papilloma cells, but lead to death by inhibiting cellular division and producing pathological changes in the cells which then continue to differentiate. The virus associated with the growths, however, not only persists in undiminished amount during regression, but often an increased yield of it can be obtained on extraction. The fibroma virus in crude extracts or in vivo is inactivated by far less irradiation than the papilloma virus. 10,000 r destroys 90 per cent or more of the infectivity of the fibroma virus, whereas at least 100,000 r is required to inactivate 50 per cent of the papilloma virus in extracts containing about the same amount of protein. No variant of the papilloma virus or fibroma virus has been encountered as a result of the irradiation.

scholarly journals Increased cytotoxicity of normal rabbit serum for lectin-resistant mutants of animal cells.

1984 ◽  
Vol 160 (4) ◽  
pp. 1241-1246
Author(s):  
C Jones
Keyword(s):  
Structural Changes ◽  
Chinese Hamster ◽  
Rabbit Serum ◽  
Cytotoxic Action ◽  
Normal Rabbit Serum ◽  
Animal Cells ◽  
Naturally Occurring ◽  
Alternate Complement Pathway ◽  
Surface Carbohydrates ◽  
Naturally Occurring Antibodies

Plant lectins are cytotoxic and can be used to select for mutants of animal cells that exhibit structural changes in cell surface carbohydrates reflecting glycosylation defects. We isolated eight lectin mutants of Chinese hamster ovary (CHO) cells that appear to represent three different phenotype classes. These lectin mutants were much more sensitive to the cytotoxic action of normal rabbit serum (NRS) than were the parental cells. This increased cytotoxicity was heat sensitive, specifically absorbed, and inhibited by simple and complex carbohydrates. No killing was observed under conditions in which only the alternate complement pathway was active. An NRS-resistant subclone that was isolated from one lectin mutant was shown to have also regained wild type behavior when tested with the lectins. The possibility that naturally occurring antibodies in rabbit serum are reacting with incomplete carbohydrate chains on the surface of the lectin mutants is discussed.

scholarly journals STUDIES ON THE MECHANISM OF THE FORMATION OF THE PENICILLIN ANTIGEN

1961 ◽  
Vol 114 (6) ◽  
pp. 875-940 ◽  
Author(s):  
Bernard B. Levine ◽  
Zoltan Ovary
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Penicillin G ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Human Beings ◽  
Mixed Disulfide ◽  
Diastereomeric Mixture ◽  
Potassium Penicillin

An excess of D-benzylpenicillenic acid (BPE) was reacted with human γ-globulin, human serum albumin, gelatin, and poly-L-lysine in aqueous solution buffered at pH 7.5–8.0. Under these conditions, BPE reacted predominantly with lysine ϵ-amino groups of the proteins to form the mixture of diastereomers of ϵ-N-(D-α-benzylpenicilloyl)-lysine groups (Di-BPO-Lys). BPE reacted also, but to a considerably smaller extent, with cystine disulfide linkages of human γ-globulin and human serum albumin to form D-benzylpenicillenic acid-cysteine mixed disulfide groups (BPE-SS-Cys). Conjugates containing large numbers of BPE or D-penicillamine mixed disulfide groups were prepared by reaction of BPE or D-penicillamine with thiolated human γ-globulin under mild oxidizing conditions. Anti-penicillin antibodies were produced in rabbits by immunization with either potassium penicillin G (PG) or a preincubated mixture of PG with normal rabbit serum (PG-NRS) in complete Freund's adjuvant. Specific precipitation analyses in aqueous and gel media (Ouchterlony), PCA analyses, and specific inhibition of these reactions with haptens were carried out on the rabbit anti-PG and anti-(PG-NRS) sera, using the above conjugates as antigens. The anti-penicillin antibodies were found to be directed against the diastereomeric mixture of N-(D-α-benzylpenicilloyl) groups, predominantly the Di-BPO-Lys groups. By these techniques, no antibodies directed against the BPE-mixed disulfide or the D-penicillamine mixed disulfide groups were detected. Three out of six patients with histories of allergic reactions to PG responded with wheal-and-erythema reactions to the N-(D-α-benzylpenicilloyl) (BPO) groups contained in BPE-human gamma globulin conjugate. Another such patient exhibited serum antibodies specific for the BPO group. One patient being treated with 25 gm per day of PG showed the presence of non-dialyzable antigenic BPO-conjugates in his serum. These results demonstrate that the diastereomeric BPO groups (predominantly Di-BPO-Lys groups) are major antigenic determinant groups responsible for PG hypersensitivity in rabbits and human beings. The possible clinical usefulness of multivalent Di-BPO conjugates and univalent Di-BPO haptens is discussed.

Central administration of alpha-MSH antiserum augments fever in the rabbit

1986 ◽  
Vol 250 (5) ◽  
pp. R803-R806 ◽  
Author(s):  
S. T. Shih ◽  
O. Khorram ◽  
J. M. Lipton ◽  
S. M. McCann
Keyword(s):  
Interleukin 1 ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Central Administration ◽  
Normal Body Temperature ◽  
Melanocyte Stimulating Hormone ◽  
Average Rise ◽  
The Brain ◽  
Antipyretic Action

alpha-Melanocyte-stimulating hormone (alpha-MSH) has a marked antipyretic action when given centrally or peripherally, and the concentration of this peptide within the septal region of the brain increases during fever. To assess the significance of endogenous central alpha-MSH in fever, antiserum was given to rabbits via a cannula implanted in the third cerebral ventricle. Each day for 3 days, the animals received 50 microliters of normal rabbit serum (NRS) or an equal volume of antiserum raised against alpha-MSH. Interleukin 1 (IL 1) was then injected intravenously to determine the effect of central immunoneutralization of alpha-MSH on the febrile response. Immunoneutralization markedly prolonged fever. The average rise in temperature and the area under the fever curve after IL 1 injection were also significantly increased. Antiserum treatment did not alter normal body temperature, and NRS had no effect on IL 1-induced fever. These results indicate that endogenous central alpha-MSH contributes to physiological limitation of fever and that the role of this peptide in temperature regulation is relevant to the febrile state but not to normothermia.

Mechanism of oleic acid-induced inhibition on gastric acid secretion in rats

1991 ◽  
Vol 260 (4) ◽  
pp. G564-G570 ◽  
Author(s):  
J. C. Rhee ◽  
T. M. Chang ◽  
K. Y. Lee ◽  
Y. H. Jo ◽  
W. Y. Chey
Keyword(s):  
Oleic Acid ◽  
Acid Secretion ◽  
Peptide Yy ◽  
Acid Output ◽  
Inhibitory Effect ◽  
Rabbit Serum ◽  
Similar Degree ◽  
Normal Rabbit Serum ◽  
Anesthetized Rats ◽  
Acid Acid

We investigated the existence of an enterogastrone in rats induced by duodenal administration of oleic acid. Acid secretion by the luminally perfused stomach was stimulated in anesthetized rats by intravenous infusion of 0.3 micrograms.kg-1.h-1 pentagastrin. Intraduodenal administration of 3 mmol of oleic acid produced a profound inhibition (94%) of pentagastrin-stimulated acid output in 10 rats (P less than 0.01). Of several peptides in plasma including secretin, neurotensin, somatostatin, and peptide YY, only secretin was found to increase significantly (P less than 0.001). A similar degree of inhibition of acid output (93%) was caused by porcine secretin, 5.6 pmol.kg-1.h-1, given intravenously to mimic the plasma level of secretin produced by oleic acid infusion. The inhibitory effect of oleic acid on the acid secretion was completely reversed by intravenous injection of a rabbit antisecretin serum but not by a normal rabbit serum. These observations strongly suggest that the inhibition was mediated via circulating secretin. The inhibition produced by either oleic acid or secretin was completely blocked by indomethacin. The blocking action was completely reversed by intravenous administration of 48 micrograms.kg-1.h-1 prostaglandin E2. We conclude that endogenous secretin is a major enterogastrone released by oleic acid in anesthetized rats and that the inhibitory action of secretin requires endogenous prostaglandins.

scholarly journals Fate of Listeria monocytogenes in Normal Rabbit Serum

1973 ◽  
Vol 7 (2) ◽  
pp. 289-297
Author(s):  
Leonard D. Shultz ◽  
Martin S. Wilder
Keyword(s):  
Listeria Monocytogenes ◽  
Rabbit Serum ◽  
Normal Rabbit Serum
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