scholarly journals THE PROTECTIVE ACTION OF TYPE I ANTIPNEUMOCOCCUS SERUM IN MICE

1936 ◽  
Vol 64 (3) ◽  
pp. 377-383 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Selective Adsorption ◽  
Protective Action ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Type I ◽  
Antibody Complex ◽  
Antigen Antibody

1. The addition of small amounts of cholesterol and of cephalin reduces markedly the protective action of antipneumococcus horse serum. 2. These lipids do not affect the protective action of antipneumococcus rabbit serum. 3. These findings may be explained (a)by the selective adsorption of lipid on the antigen-antibody complex, and (b) by certain lipid antagonisms. 4. The failure of large amounts of immune horse serum to protect mice against pneumococcus infection is explicable on the basis of selective participation of lipids dependent upon the species from which the antibody is derived. 5. The lipids modify the results of protection tests only through participation in the process of specific sensitization.

scholarly journals THE PROTECTIVE ACTION OF TYPE I ANTIPNEUMOCOCCUS SERUM IN MICE

1936 ◽  
Vol 64 (3) ◽  
pp. 369-375 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Characteristic Property ◽  
Protective Action ◽  
Horse Serum ◽  
The Other ◽  
Rabbit Serum ◽  
Type I ◽  
Infectious Process ◽  
Marked Inhibition ◽  
Secondary Factor ◽  
Antigen Antibody

1. Type I antipneumococcus horse serum, in amounts exceeding a characteristic optimum, fails to protect mice against infection with the homologous type pneumococci. This failure is due to a marked inhibition of the phagocytic mechanism in the earlier stages of the infectious process. On the other hand, antipneumococcus rabbit serum in similar quantities does not inhibit phagocytosis, nor does it block the protection. 2. The experimental evidence suggests that the prozoning action of immune horse serum is due primarily to some characteristic property of the specific antibody and secondarily to an heterologous component of the serum, ineffective in itself but acting through the mediation of the antigen-antibody combination. This secondary factor may be a lipid.

scholarly journals THE EFFECT OF ANTISERUM, ALONE AND WITH HYDROCORTISONE, ON FOETAL MOUSE BONES IN CULTURE

1965 ◽  
Vol 121 (4) ◽  
pp. 551-560 ◽  
Author(s):  
Honor B. Fell ◽  
L. Weiss
Keyword(s):  
Lysosomal Enzymes ◽  
Protective Action ◽  
Rabbit Antiserum ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Limb Bones ◽  
Mouse Tissues ◽  
Antigen Antibody ◽  
Indirect Action

1. The effects of normal rabbit serum and of rabbit antiserum to whole foetal mouse tissues, on the isolated limb bones of late foetal mice were studied in organ culture, and the influence of hydrocortisone on these effects was investigated. 2. Unheated normal serum caused slight loss of metachromatic material from the cartilage matrix, and some resorption of both cartilage and bone. 3. In unheated antiserum to foetal mouse tissues, the terminal cartilage was smaller and less metachromatic than in paired controls in normal serum, while osteoclasis was so intense that in many explants the bone had almost disappeared. The amount of necrosis varied with different batches of antiserum. 4. The changes produced by normal serum and antiserum could be largely prevented by heating the sera to 57°C for 45 minutes. 5. The effects could also be inhibited by the addition of hydrocortisone to the unheated sera; as little as 0.1 µg hydrocortisone per ml of medium had a well marked protective action. 6. It is suggested that (a) unheated antiserum causes a release of lysosomal enzymes with consequent breakdown of intercellular material, (b) this release is due to an indirect action on the lysosome via an increased permeability of the cell membrane, (c) hydrocortisone does not affect the antigen-antibody reaction, but inhibits the autolytic changes that normally follow this reaction, possibly by stabilising both the lysosomal and cell membranes.

scholarly journals STUDIES ON PHOTO-OXIDATION OF ANTIGEN AND ANTIBODIES

1941 ◽  
Vol 73 (2) ◽  
pp. 223-242 ◽  
Author(s):  
Hans Smetana ◽  
David Shemin
Keyword(s):  
Specific Antibody ◽  
Horse Serum ◽  
Amino Nitrogen ◽  
Rabbit Serum ◽  
Type I ◽  
Egg Albumin ◽  
Photo Oxidation ◽  
Precipitin Reaction ◽  
Antigenic Properties ◽  
Chemical Studies

1. Quantitative precipitin studies indicate that progressive photo-oxidation progressively destroys the antigenic function of egg albumin. 2. Quantitative precipitin reactions of antisera (anti-egg albumin rabbit serum and antipneumococcus Type I horse serum) demonstrate that progressive photo-oxidation causes progressive lowering of the potency of the sera. 3. Quantitative precipitin reactions of the photo-oxidized globulin gamma fraction of anti-egg albumin rabbit serum and of Felton solution of antipneumococcus Type I horse serum show that these specific antibody fractions behave similarly to antibodies in whole sera. 4. Egg albumin whose precipitin reaction is destroyed by photo-oxidation no longer causes anaphylaxis in guinea pigs and does not produce precipitins in rabbits. 5. Chemical studies of progressively photo-oxidized egg albumin show a progressive destruction of tryptophane and histidine while tyrosine remains intact and cystine is reversibly oxidized. Sulfhydryl groups can no longer be demonstrated in photo-oxidized egg albumin whose antigenic characteristics are greatly weakened. 6. Similar studies on the globulin gamma fraction of anti-egg albumin rabbit serum and on Felton solution show no diminution of these amino acids in photo-oxidized material whose antigenic properties are destroyed. 7. The non-coagulable nitrogen and the amino nitrogen of egg albumin, antisera, and their specific antibody fractions show but an insignificant increase during photo-oxidation, indicating that the loss of the precipitin reaction is not due to splitting of the respective protein molecules. 8. Electrophoretic studies of egg albumin, antisera, and their specific antibody fractions show that photo-oxidation causes a marked alteration of the pattern of these substrates. 9. Photo-oxidation of proteins causes the formation of aggregates, indicating denaturation. 10. Hematoporphyrin migrates with the albumin fraction of unaltered as well as the photo-oxidized anti-egg albumin rabbit serum and pneumococcus Type I horse serum; in isolated proteins such as egg albumin, globulin gamma, or Felton solution, etc., the dye moves independently of the protein; after progressive photo-oxidation Hp becomes progressively fixed to the protein. Eosin behaves similarly to hematoporphyrin.

scholarly journals CRYSTALLINE PNEUMOCOCCUS ANTIBODY

1949 ◽  
Vol 32 (6) ◽  
pp. 705-724 ◽  
Author(s):  
John H. Northrop ◽  
Walther F. Goebel
Keyword(s):  
Ammonium Sulfate ◽  
Horse Serum ◽  
Insoluble Fraction ◽  
Rabbit Serum ◽  
Type I ◽  
Type Ii ◽  
Serum Globulin ◽  
Saturated Ammonium Sulfate ◽  
Diphtheria Antitoxin ◽  
Specific Polysaccharide

1. The immune precipitate formed by antipneumococcus horse serum and the specific polysaccharide is not hydrolyzed by trypsin as is the diphtheria toxin-antitoxin complex, and purified pneumococcus antibody cannot be isolated by the method used for the isolation and crystallization of diphtheria antitoxin. 2. Type I pneumococcus antibody, completely precipitable by Type I polysaccharide, may be obtained from immune horse serum globulin by precipitation of the inert proteins with acid potassium phthalate. 3. The antibody obtained in this way may be fractionated by precipitation with ammonium sulfate into three main parts. One is insoluble in neutral salts but soluble from pH 4.5 to 3.0 and from pH 9.5 to 10.5. This is the largest fraction. A second fraction is soluble in 0.05 to 0.2 saturated ammonium sulfate and the third fraction is soluble in 0.2 saturated ammonium sulfate and precipitated by 0.35 saturated ammonium sulfate. The second fraction can be further separated by precipitation with 0.17 saturated ammonium sulfate to yield a small amount of protein which is soluble in 0.17 saturated ammonium sulfate but insoluble in 0.25 saturated ammonium sulfate. This fraction crystallizes in poorly formed, rounded rosettes. 4. The crystallization does not improve the purity of the antibody and is accompanied by the formation of an insoluble protein as in the case of diphtheria antitoxin. 5. None of the fractions obtained is even approximately homogeneous as determined by solubility measurements. 6. Purified antibody has also been obtained by dissociating the antigen-antibody complex. 7. The protective value of the fractions is quite different; that of the dissociated antibody being the highest and that of the insoluble fraction, the lowest. 8. All the fractions are immunologically specific since they do not precipitate with Type II polysaccharide nor protect against Type II pneumococci. 9. All the fractions give a positive precipitin reaction with antihorse rabbit serum. The dissociated antibody gives the least reaction. 10. Comparison of the various fractions, either by their solubility in salt solution or through immunological reactions, indicates that there are a large number of proteins present in immune horse serum, all of which precipitate with the specific polysaccharide but which have very different protective values, different reactions with antihorse rabbit serum, and different solubility in salt solutions.

STUDIES ON A THYROID STIMULATING FACTOR IN URINARY CHORIONIC GONADOTROPHIN PREPARATIONS

1967 ◽  
Vol 55 (4) ◽  
pp. 587-599 ◽  
Author(s):  
A. Burger ◽  
R. Kunz
Keyword(s):  
Biological Response ◽  
Chorionic Gonadotrophin ◽  
Rabbit Serum ◽  
Soluble Antigen ◽  
Globulin Fraction ◽  
Human Pituitary ◽  
Antibody Complex ◽  
Antigen Antibody ◽  
Stimulating Factor ◽  
Immune Rabbit

ABSTRACT Thyroid stimulating activity was demonstrated in human urinary chorionic gonadotrophin preparations (HCG) by the method of McKenzie (1958). The biological response of the material was similar to that of bovine pituitary thyrotrophin (TSH), but no neutralization of the activity occurred with antibodies against human pituitary TSH and, even more interesting, with antibodies against human urinary chorionic gonadotrophin preparations. The latter antibodies perfectly neutralized human pituitary TSH. The Gamma-G-globulins precipitated from a mixture of HCG and anti-HCG contained biological activity whereas no activity was recovered in the Gamma-G-globulin fraction when HCG was mixed with non immune rabbit serum. This may indicate the presence of a soluble antigen-antibody complex.

scholarly journals QUANTITATIVE EXPERIMENTS WITH ANTIBODIES TO A SPECIFIC PRECIPITATE. I

1941 ◽  
Vol 73 (1) ◽  
pp. 125-140 ◽  
Author(s):  
Henry P. Treffers ◽  
Michael Heidelberger
Keyword(s):  
Horse Serum ◽  
Serum Antibody ◽  
Protein Molecule ◽  
Antigenic Specificity ◽  
Rabbit Serum ◽  
Type I ◽  
Egg Albumin ◽  
Homologous Antigen ◽  
Antibody Function ◽  
Immune Rabbit

1. Rabbits were injected with the washed specific precipitate from Type II antipneumococcus horse serum. Antibody in the resulting antiserum was determined by the quantitative agglutinin method using various specific precipitates as antigens. 2. Suspensions of Types I and II antipneumococcus horse specific precipitates, as well as the specific precipitates derived from Type VIII Pn (anti-C portion), and H. influenzae horse antisera were found to remove the same amount of antibody from the immune rabbit serum. 3. Purified antibody solutions prepared by dissociation methods from Types I and II antipneumococcus horse sera were found to remove the same quantity of antibody as did the homologous specific precipitates. 4. Specific precipitates from anti-crystalline egg albumin and anti-diphtheria horse sera were found to remove only a fraction of the antibody. The reasons for this are discussed. 5. A specific precipitate prepared from pepsin-digested Type I anti-pneumococcus horse serum removed all of the antibody to the homologous antigen from the rabbit anti-precipitate serum, but followed a different quantitative course. 6. From the quantitative course of these reactions and from experiments with specific precipitates from anti-Pn rabbit and pig sera it is concluded that the only antigenic specificity demonstrable for the antibodies investigated was that due to their common origin, and that the groupings responsible for their antibody function constitute either a small part of the total protein molecule or else are non-antigenic.

scholarly journals STUDIES ON IMMUNOLOGICAL RELATIONSHIPS AMONG THE PNEUMOCOCCI

1929 ◽  
Vol 49 (2) ◽  
pp. 183-193 ◽  
Author(s):  
John Y. Sugg ◽  
James M. Neill
Keyword(s):  
Horse Serum ◽  
Rabbit Serum ◽  
Type I ◽  
Type Ii ◽  
Immunological Relationship ◽  
The Individual ◽  
Relationship Of ◽  
Convincing Data

The paper reports evidence of an immunological relationship between one variety of Saccharomyces ceremsise and the Type II variety of Diplococcus pneumonix (Pneumococcus). The most convincing data consisted of the reactions of the Type II bacteria with potent antiyeast serum which agglutinated, and protected mice against these pneumococci as well as the average antiserum obtained by immunization of rabbits with Type II bacteria themselves. The reactivity of the antiyeast serum is strictly specific to the Type II variety of Pneumococcus in the sense that it is entirely devoid of antibodies reactive with Type I or III. The results of absorption experiments with both the antiyeast (rabbit) serum and the anti-Type II (horse) serum were the same as those usually obtained in analogous experiments with immunologically related, but not identical, kinds of bacteria. The immunological relationship of the yeast and the Type II pneumococcus is apparently based upon S-anti-S reactions. It represents an example of heterogenetic specificity which is of particular interest because of the wide genetic separation of the pathogenic schizomycete and the saprophytic ascomycete. Data on the individual irregularity in the yeast-agglutinating capacity of serum from non-immunized or "normal" rabbits are presented as experimental facts.

scholarly journals LIPOIDS AND IMMUNOLOGICAL REACTIONS

1935 ◽  
Vol 62 (4) ◽  
pp. 485-503 ◽  
Author(s):  
Frank L. Horsfall ◽  
Kenneth Goodner
Keyword(s):  
Specific Antibody ◽  
Marked Reduction ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Type I ◽  
Initial Activity ◽  
Immunological Reactions ◽  
Specific Reactions

It has been demonstrated that the removal of lipoids from Type I antipneumococcus horse serum causes a loss of the visible phenomena of type specific agglutination and precipitation, and in the case of rabbit serum a marked reduction in these properties. Initial activity of the type specific antibody can be restored to extracted immune horse serum by the addition of lecithin, and to rabbit serum by the addition of cephalin. The significance of these observations in respect to the relation of phospholipins to the type specific reactions of antipneumococcus serum is discussed.

scholarly journals THE COMPLEMENT FIXATION REACTION WITH PNEUMOCOCCUS CAPSULAR POLYSACCHARIDE

1936 ◽  
Vol 64 (2) ◽  
pp. 201-216 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Capsular Polysaccharide ◽  
Complement Fixation ◽  
Selective Adsorption ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Negative Results ◽  
Fixation Reaction ◽  
Immune Aggregates ◽  
Positive Results ◽  
Immune Rabbit

1. Complement is not fixed by immune aggregates resulting from the interaction of pneumococcus capsular polysaccharide and type-specific immune horse serum, although under proper conditions the substitution of immune rabbit serum gives positive results. 2. The negative results with immune horse serum are due to some poorly understood property of the specific antibodies rather than to some heterologous inhibitor present in the serum. 3. It has been shown that with immune rabbit serum-polysaccharide combinations, complement fixation is an adsorptive phenomenon conditioned upon the surface exposure of the immune aggregates. 4. A close parallelism to the selective adsorption of phosphatides by these immune aggregates has been pointed out. 5. In those instances in which complement is fixed this phenomenon must be regarded as tertiary and conditioned by (a) union of antigen and antibody, and (b) particulation. 6. The general significance of complement fixation as applied to bacterial polysaccharides has been discussed.

scholarly journals THE PNEUMOCOCCAL CAPSULAR SWELLING REACTION, STUDIED WITH THE AID OF THE ELECTRON MICROSCOPE

1943 ◽  
Vol 78 (5) ◽  
pp. 327-332 ◽  
Author(s):  
Stuart Mudd ◽  
Ferdinand Heinmets ◽  
Thomas F. Anderson
Keyword(s):  
Capsular Polysaccharide ◽  
Specific Antigen ◽  
Immune Serum ◽  
Rabbit Serum ◽  
Surface Deposit ◽  
Specific Serum ◽  
Antibody Complex ◽  
Wall Interaction ◽  
Antigen Antibody ◽  
Serum Components

Electron micrographs indicate, in harmony with previous findings, that the pneumococcal capsule is a gel of low density outside of and closely applied to the bacterial cell wall. Interaction with homologous immune rabbit serum greatly increases the thickness and density of this capsular gel; the increase in thickness of the specifically swollen pneumococcal capsule may exceed by 25-fold the thickness of the surface deposit caused by rabbit immune serum on the cell walls and flagella of homologous non-capsulated bacteria. Conclusions drawn from these and earlier data are that homologous immune serum permeates the pneumococcal capsular gel; the specific antibody combines with the capsular polysaccharide; non-specific serum components are secondarily adsorbed to or combined with the specific antigen-antibody complex. The relatively low antibacterial titers characteristic of pneumococcal antisera can be explained in part by the permeation of the capsule by antiserum, in part by the high combining capacity of pneumococcal carbohydrate for antibody (17).

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