scholarly journals THE INFLUENCE OF INFLAMMATION ON THE ABSORPTION OF SUBSTANCES OF VARIED DIFFUSIBILITY

1938 ◽  
Vol 67 (4) ◽  
pp. 619-641 ◽  
Author(s):  
Rose G. Miller
Keyword(s):  
Peritoneal Cavity ◽  
Subcutaneous Tissue ◽  
Horse Serum ◽  
Type I ◽  
Phenol Red ◽  
Serum Globulin ◽  
Egg Albumin ◽  
Specific Polysaccharide ◽  
Phenol Blue ◽  
Pneumococcus Type

1. Inflammation retards the absorption of horse serum globulin and crystalline egg albumin from the peritoneal cavity and subcutaneous tissue, but retardation of the absorption of crystalline egg albumin is less than that of globulin, which is less diffusible. 2. Inflammation retards the absorption of the specific polysaccharide of pneumococcus Type I from the peritoneal cavity; inflammation may accelerate, but does not hinder, the absorption of glucose from the peritoneal cavity. 3. Inflammation retards the spread of trypan blue in the skin, but accelerates absorption from the skin of the more diffusible dye, brom phenol blue. 4. Phenol red is excreted in the urine with equal rapidity after injection into normal and into inflamed subcutaneous tissue or into normal and into inflamed peritoneal cavities. Direct extractions of phenol red from inflamed subcutaneous sites indicate that inflammation accelerates the absorption of the dye from these areas. 5. Inflammation retards the absorption of the indiffusible proteins, carbohydrates and dyes; it tends to accelerate the absorption of the diffusible carbohydrates and dyes.

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 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 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 IMMUNOCHEMICAL PROPERTIES OF NATIVE AND DENATURED HORSE SERUM GLOBULINS

1945 ◽  
Vol 28 (5) ◽  
pp. 421-448 ◽  
Author(s):  
John O. Erickson ◽  
Hans Neurath
Keyword(s):  
Horse Serum ◽  
Guanidine Hydrochloride ◽  
Specific Effect ◽  
Cross Reactivity ◽  
Type I ◽  
Serum Globulin ◽  
Antigenic Activity ◽  
Order Of Magnitude ◽  
The Mean ◽  
Mean Molecular Weight

1. The influence of guanidine hydrochloride on the denaturation and regeneration of Type I antipneumococcal horse serum globulin was determined by measurements of viscosity, diffusion, and sedimentation in the ultracentrifuge. In addition, the effect of NaCNS on the antibody globulin was studied. 2. Both the irreversibly denatured and the regenerated fractions were found to be precipitable by SI. The observed changes in combining ratio have been tentatively explained in terms of (a) changes in the mean molecular weight, or alternatively (b) an increase in the number of serologically active groups upon denaturation, followed by masking of the latter upon regeneration. Discounting a specific effect of NaCNS on either fraction, the extent of specific precipitation is of the same order of magnitude for native and irreversibly denatured antibody. 3. Quantitative precipitin titrations have been performed on rabbit antisera to native and irreversibly denatured horse antibody, and normal globulin GI, respectively. No significant differences in the antigenic activity of these proteins were found. Measurements of their cross-reactivity led to the conclusion that the native and irreversibly denatured fractions of antibody globulin are antigenically more closely related to each other than to the corresponding fractions of normal globulin, and vice versa.

scholarly journals IMMUNOLOGICAL STUDIES ON A NEW PREPARATION OF TYPE SPECIFIC POLYSACCHARIDE FROM PNEUMOCOCCUS TYPE I

1936 ◽  
Vol 64 (6) ◽  
pp. 843-854 ◽  
Author(s):  
Bacon F. Chow
Keyword(s):  
Alkaline Medium ◽  
Slight Modification ◽  
Passive Immunity ◽  
Rabbit Serum ◽  
Type I ◽  
Specific Polysaccharide ◽  
Immune Rabbit ◽  
Pneumococcus Type

A type specific polysaccharide has been isolated from the autolyzed broth of Type I Pneumococcus by a modified Avery and Goebel's method. The newly prepared polysaccharide reacts with the homologous immune rabbit serum which has been completely absorbed with the acetyl polysaccharide of Avery and Goebel. The newly prepared polysaccharide produces passive immunity in mice and rats and possibly in rabbits. The antigenicity is not lost on boiling in acid or alkaline medium, but the precipitative activity is decreased. In conclusion, it has been shown that the polysaccharide from Type I Pneumococcus, as isolated by a slight modification of Avery and Goebel's method, is a more complete antigen.

scholarly journals SEROLOGICAL RELATIONSHIP BETWEEN PNEUMOCOCCUS TYPE I AND AN ENCAPSULATED STRAIN OF ESCHERICHIA COLI

1935 ◽  
Vol 62 (2) ◽  
pp. 281-287 ◽  
Author(s):  
L. A. Barnes ◽  
Eleanor C. Wight
Keyword(s):  
Escherichia Coli ◽  
Horse Serum ◽  
Rabbit Serum ◽  
Type I ◽  
Type B ◽  
Soluble Substance ◽  
Serological Relationship ◽  
Normal Horse Serum ◽  
The Relationship ◽  
Pneumococcus Type

An encapsulated strain of Escherichia coli has been isolated which is hemolytic, pathogenic for mice, and which has served to illustrate further evidence of heterogenetic specificity. The relationship appears to be limited to the serological reactions between the colon organism and Type I antipneumococcic horse serum. Type I antipneumococcic rabbit serum failed to agglutinate the organism and no reactions occurred with Types II and III antipneumococcic horse serums, normal horse serum, and a variety of other immune horse serums. Serum from rabbits immunized with the colon bacillus agglutinated the homologous organism and precipitated its soluble substance, but failed to cause agglutination of Type I pneumococci or to precipitate Type I pneumococcic polysaccharide. The evidence indicates a connection somewhat analogous to that between Type II pneumococcus and Type B Friedländer's bacillus.

scholarly journals STUDIES ON EXPERIMENTAL PNEUMONIA

1920 ◽  
Vol 32 (1) ◽  
pp. 1-18 ◽  
Author(s):  
Russell L. Cecil ◽  
Francis G. Blake
Keyword(s):  
Beneficial Effect ◽  
Therapeutic Effect ◽  
Intravenous Injection ◽  
Horse Serum ◽  
Type I ◽  
Experimental Pneumonia ◽  
Normal Horse Serum ◽  
Lethal Doses ◽  
Pneumococcus Type

1. In experimental Pneumococcus Type I pneumonia in monkeys the intravenous injection of Type I antipneumococcus serum exercises a specific therapeutic effect, frees the blood promptly and permanently from pneumococci, shortens the course of the disease, and greatly moderates its severity. Of five monkeys inoculated intratracheally with lethal doses of Pneumococcus Type I, all developed pneumonia, and all recovered following the administration of Type I antipneumococcus serum, while the controls died. 2. The earlier the serum is administered the shorter and less severe the pneumonia. Frequent injections are also an important factor in obtaining favorable results. When serum treatment is instituted late in the disease, the injections must usually be continued over a longer period of time in order to achieve success. 3. Normal horse serum exerts no beneficial effect whatever in experimental Pneumococcus Type I pneumonia.

scholarly journals CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION

1936 ◽  
Vol 63 (5) ◽  
pp. 737-744 ◽  
Author(s):  
Michael Heidelberger ◽  
Elvin A. Kabat
Keyword(s):  
Specific Antibody ◽  
Horse Serum ◽  
The Other ◽  
Type I ◽  
Specific Polysaccharide ◽  
Chemical Studies ◽  
The Absolute ◽  
Bacterial Agglutination

1. The absolute, quantitative agglutinin method has been used for the determination of the presence or absence of small amounts of specific polysaccharide in pneumococcus variants. 2. A technique is described for the removal of group specific antibody from antipneumococcus horse serum. 3. The type specific anticarbohydrate agglutinin and precipitin are not only present in identical amounts in Type I antipneumococcus horse serum, but a reduction in one is also accompanied by a quantitatively identical reduction in the other, providing evidence for their actual identity. In purified antibody solutions somewhat more agglutinin than precipitin is found, possibly owing to alteration of a portion of the antibody in the process of purification.

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