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 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 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.

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 The formation of precipitates on mixing anti-horse sera

1950 ◽  
Vol 48 (1) ◽  
pp. 52-72
Author(s):  
G. R. E. Naylor
Keyword(s):  
Horse Serum ◽  
The Other ◽  
Homologous Antigen ◽  
Single Antigen ◽  
Antibody Reaction ◽  
Antigen Antibody

1. Five anto-horse sera which did not contain antibodies for horse-serum crystalbumin have been shown by absorption experiments to contain horse-serum crystalbumin.2. All five sera precipitated when mixes with other anti-horse sera containing anti-crystalbumin, precipitation being due to the presence of horse-serum crystalbumin in one antiserum and of anti-crystalbumin in the other.3. Antigen and its homologous antibody were never found together in the serum of an animal, and contradictory results in other experiments are probably due to impure multiple antigens.4. It is concluded that anti-horse sera may contain some of the antigenic components of injected horse serum together with antibodies to other antigens of the horse serum, but not homologous antigen and antibody. Consequently, the ‘mutual’ precipitation of anti-horse sera is due to the presence of a number of antigens in horse serum, one or more of which, present in one anti-horse serum, in the absence of its homologous antibody, may precipitate when mixed with another anti-horse serum which contains the homologous antibody.5. The use in these experiments of a single α-procedure optimum as the indicator of an antigen-antibody reaction illustrates a method enabling the investigation of problems involving single antigen-antibody reactions, even though the available reagents consist of mistures of antigens and mixtures of antibodies.

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 ENHANCEMENT OF THE OPSONIZING AND AGGLUTINATING POWERS OF ANTIPNEUMOCOCCUS SERUM BY SPECIFIC PRECIPITATING SERUM

1920 ◽  
Vol 32 (3) ◽  
pp. 283-293 ◽  
Author(s):  
Ida W. Pritchett
Keyword(s):  
Horse Serum ◽  
Test Tube ◽  
Immune Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Type I ◽  
Type Ii ◽  
Normal Horse Serum ◽  
Serum Type

1. No demonstrable antiopsonins are formed in rabbits following the intravenous injection of monovalent pneumococcus horse sera, Types I, II, and III. 2. The serum of rabbits injected with immune pneumococcus horse serum, Type I, II, or III, or with normal horse serum, when mixed in the proportion of 1:4 with Type I or Type II pneumococcus horse serum, can greatly augment, in vitro, the opsonization and agglutination of Type I and Type II pneumococci by the homologous immune horse sera. No similar effect is obtained with Type III serum and pneumococci. 3. The increase in opsonization and agglutination is dependent upon (a) specific sensitization of the pneumococci by the homologous immune serum and (b) the presence of the precipitating serum. In the absence of sensitization, as when a heterologous or normal horse serum is employed, opsonization and agglutination do not occur, even though a precipitating mixture is provided. The substitution of normal rabbit serum for the precipitating rabbit serum gives opsonization and agglutination in dilutions slightly higher than are effected with salt solution only, due possibly to the more favorable medium created for the leucocytes by the addition of 25 per cent of whole rabbit serum. 4. Different methods of combining the immune horse serum, precipitating rabbit serum, and pneumococci yield very similar results, preliminary sensitization of the bacteria before precipitation, or precipitation in the rabbit-horse serum mixture before the addition of the pneumococci for sensitization causing little if any difference in result from that obtained when immune horse serum, precipitating rabbit serum, and pneumococci are all mixed and incubated together. 5. This increased opsonization in the test-tube does not seem to be paralleled by increased protective power, or at any rate such protection is not readily demonstrated.

scholarly journals PROPERTIES OF THE TYPE SPECIFIC PROTEINS OF ANTIPNEUMOCOCCUS SERA

1937 ◽  
Vol 66 (4) ◽  
pp. 425-435 ◽  
Author(s):  
Kenneth Goodner ◽  
Frank L. Horsfall
Keyword(s):  
Capsular Polysaccharide ◽  
Horse Serum ◽  
Total Content ◽  
Immune Serum ◽  
Rabbit Serum ◽  
Antibody Activity ◽  
Subsequent Paper ◽  
Type I ◽  
Protective Capacity ◽  
Precipitable Protein

The generally held view has been that in any immune serum only a single antibody would be induced by and react with a single antigen. Were this true the various manifestations of antibody activity should show a quantitative parallelism. It has already been shown (1), however, that with antipneumococcus horse serum the mouse protective potency does not parallel the maximum amount of specifically precipitable protein except within certain well defined groups of antisera. The simplest explanation of this situation is that different horses form antibodies differing in specific protective capacity, but from our studies it seems probable that in any immune serum there may occur a mixture of antibodies which, while directed against the same antigen, possess different protective capacities, different avidities, etc. It would now appear that this latter hypothesis is the more tenable since the experiments here reported indicate the existence of antibodies of various protective potencies in horse antisera. It would not be unreasonable to hold that the antibodies of a single serum represent a series of substances with varying properties. On the basis of the present immunological fractionation experiments, the following deductions seem permissible. 1. Antipneumococcus horse sera must contain at least three, possibly many, antibody substances which react with the capsular polysaccharide. These are: (a) A substance which precipitates upon the addition of a relatively small amount of polysaccharide. This antibody possesses a low protective potency. (b) A substance which is precipitated with intermediate amounts of polysaccharide and which possesses an extremely high protective value. (c) A third substance which is precipitated only with the addition of relatively large amounts of polysaccharide. The protective value of this antibody is very low It may represent a degraded form. 2. With antipneumococcus rabbit serum the situation is somewhat simpler. This is in accord with the fact that with Type I antipneumococcus sera from this species there is a direct proportionality between the amount of specifically precipitable protein and the protective potency of the serum (1). The results with antipneumococcus rabbit serum indicate the existence of at least two antibody substances: (a) An antibody with high protective value which makes up the greater proportion of the total content. (b) A second substance which is precipitated only upon the addition of relatively large amounts of capsular polysaccharide. The existence of this second antibody is not clearly demonstrated by the present findings but the lower protective ratios obtained as greater amounts of antibody are removed probably indicate its existence. This may also represent degraded material. The observations on the antibodies of both horse and rabbit antisera will be supported by experiments with immunochemical fractionation which will be reported in a subsequent paper.

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