scholarly journals CROSS-REACTIONS OF ANTITYPHOID AND ANTIPARATYPHOID B HORSE SERA WITH VARIOUS POLYSACCHARIDES

1956 ◽  
Vol 104 (3) ◽  
pp. 375-382 ◽  
Author(s):  
Michael Heidelberger ◽  
Felix Cordoba
Keyword(s):  
Acetic Acid ◽  
Horse Serum ◽  
Type Ii ◽  
Branch Points ◽  
Cross Reactions ◽  
Tamarind Seed ◽  
End Groups ◽  
Specific Polysaccharide ◽  
Fine Structures

A study was made of cross-reactions of synthetic polyglucose and of numerous plant and bacterial gums in an antityphoid and an antiparatyphoid B horse serum. The observed differences permit conclusions to be drawn regarding certain of the linkages likely to be found in the fine structures of each of the corresponding Salmonella polysaccharides:— 1. Cross-reactions of the antityphoid serum with the specific polysaccharide of Type II pneumococcus and with tamarind seed polysaccharide, glycogen and synthetic polyglucose indicate that the acetic acid-degraded O-polysaccharide of S. typhi, strain O 901, may contain part, at least, of its glucose as 1,4,6-branch points or in 1,6-linkage, perhaps adjacent to a terminal, non-reducing, galactopyranose unit. 2. Cross-reactions of both antisera with arabogalactans point to the existence of (probably ß-) 1,3-, 1,6-, and/or 1,3,6-linkages of galactose in both the typhoid and paratyphoid B polysaccharides. 3. The differential reactivities of the galactomannans and yeast mannan suggest that the mannose in the typhoid polysaccharide is linked 1,2- or 1,3- with possible non-reducing mannopyranose end groups attached 1,6-. In the paratyphoid B polysaccharide the linkages are probably galacto-oligomannose 1,4-, or 1,4,6-, or the corresponding linkages of mannose alone.

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 THE IMMUNOLOGICAL SPECIFICITY OF TYPE II PNEUMOCOCCUS AND ITS SEPARATION INTO PARTIAL SPECIFICITIES

1956 ◽  
Vol 103 (2) ◽  
pp. 189-197 ◽  
Author(s):  
Michael Heidelberger ◽  
John Adams
Keyword(s):  
Quantitative Data ◽  
Capsular Polysaccharide ◽  
Glucuronic Acid ◽  
Gum Arabic ◽  
Partial Hydrolysis ◽  
Type Ii ◽  
Branch Points ◽  
Tamarind Seed ◽  
Immunological Specificity ◽  
Multiple Units

The specificity of Type II pneumococcus determined by its capsular polysaccharide (S II) may be separated into three partial specificities, each characteristic of one of the three component sugars of S II, namely, glucuronic acid, glucose, and rhamnose. By far the largest portion of antibodies in Type II antipneumococcus horse sera which cross-react with carbohydrates containing one or more of these sugars are reactive with those characterized by multiple groupings of glucuronic acid. This confirms, extends, and explains earlier observations. In confirmation of predictions based upon existing information tamarind seed polysaccharide (jellose), in which much of the glucose exists as 1,4,6-branch points, was found to react in Type II antisera. Several instances are given of cross-reactions in these antisera apparently due to the L-rhamnose component of the reacting polysaccharides. The antisera contain far more antibody capable of precipitating with substances with multiple units of glucuronic acid than with those so far tested containing multiple 1,4,6-branch points of glucose or multiple groupings of rhamnose. The long known increase of titer of gum arabic on partial hydrolysis is now fully explained and discussed, and a chemical picture is given of the change in "avidity." The sum of the partial specificities measured does not equal the whole. Quantitative data illustrating these points are given.

scholarly journals PREDICTED AND UNPREDICTED CROSS-REACTIONS OF AN ACETYLPHOSPHOGALACTAN OF SPOROBOLOMYCES YEAST

1968 ◽  
Vol 128 (1) ◽  
pp. 189-196 ◽  
Author(s):  
Michael Heidelberger ◽  
Morey E. Slodki
Keyword(s):  
Quantitative Data ◽  
Horse Serum ◽  
Teichoic Acid ◽  
Cross Reaction ◽  
Cross Reactions ◽  
Reduced Products ◽  
End Groups ◽  
Acetyl Group

The teichoic acid of streptococcal Group N, with end groups of galactose phosphate, had been shown to cross-react with antipneumococcal sera of types VI, XIV, XVI, and XXVII. End groups of D-galactose-1-phosphate in the phosphogalactans of Sporobolomyces yeasts made it predictable that these galactans would precipitate the same antipneumococcal sera and also antisera to streptococcal Group N. The predictions were verified, and other unpredicted reactions were found. Precipitation of much of the antibody in an antipneumoccal type XVIII horse serum was shown to be due to O-acetyl-D-galactose residues in the phosphogalactan, in accord with earlier information that an O-acetyl sugar was a principal determinant of S XVIII. The new results identify this sugar as D-galactose. Since it is linked 1,3- in S XVIII, the O-acetyl group in the Sporobolomyces galactan is probably also on a 1,3-linked residue. Another major cross-reaction in anti-S. paratyphi A serum characterizes the galactose residues in the "O" polysaccharide of the bacillus as members of the D-series probably linked in tandem 1,6-, 1,6-; 1,6-, 1,3-; 1,3-, 1,6-; or 1,3-, 1,3-. Reactions of periodate-oxidized-reduced products confirm the conclusions stated above. Quantitative data are given.

scholarly journals Design, Synthesis and Biological Evaluation of N4-Sulfonamido-Succinamic, Phthalamic, Acrylic and Benzoyl Acetic Acid Derivatives as Potential DPP IV Inhibitors

2013 ◽  
Vol 7 (1) ◽  
pp. 39-48 ◽  
Author(s):  
Reema Abu Khalaf ◽  
Ghassan Abu Sheikha ◽  
Mahmoud Al-Sha'er ◽  
Mutasem Taha
Keyword(s):  
Acetic Acid ◽  
Type Ii Diabetes Mellitus ◽  
Biological Evaluation ◽  
Diabetic Patients ◽  
Type Ii ◽  
Design Synthesis ◽  
Multifunctional Protein ◽  
Design And Synthesis ◽  
Dpp Iv

As incidence rate of type II diabetes mellitus continues to rise, there is a growing need to identify novel therapeutic agents with improved efficacy and reduced side effects. Dipeptidyl peptidase IV (DPP IV) is a multifunctional protein involved in many physiological processes. It deactivates the natural hypoglycemic incretin hormone effect. Inhibition of this enzyme increases endogenous incretin level, incretin activity and should restore glucose homeostasis in type II diabetic patients making it an attractive target for the development of new antidiabetic drugs. One of the interesting reported anti- DPP IV hits is Gemifloxacin which is used as a lead compound for the development of new DPP IV inhibitors. In the current work, design and synthesis of a series of N4-sulfonamido-succinamic, phthalamic, acrylic and benzoyl acetic acid derivatives was carried out. The synthesized compounds were evaluated for their in vitro anti-DPP IV activity. Some of them have shown reasonable bioactivity, where the most active one 17 was found to have an IC50 of 33.5 μM.

Statistical Model Explaining the Fine Structure and Interface Reference of Localized Excitons in Type-II GaAs/AlAs Superlattices

1998 ◽  
Vol 07 (01) ◽  
pp. 13-35 ◽  
Author(s):  
M. V. Belousov ◽  
A. Yu. Chernyshov ◽  
I. V. Ignatev ◽  
I. E. Kozin ◽  
A. V. Kavokin ◽  
...  
Keyword(s):  
Statistical Model ◽  
Energy State ◽  
Integer Number ◽  
Type Ii ◽  
Interface Quality ◽  
Alas Layer ◽  
Densities Of States ◽  
Fine Structures ◽  
Localized Excitons

Raman scattering experiments have allowed the determination of the spatial distribution of the thicknesses of GaAs and AlAs layers in a gradient GaAs/AlAs superlattice. A statistical model is developed which is consistent with all the data and ways to improve interface quality are suggested. The fine structures of XΓ and ΓΓ excitons observed in photoluminescence and differential reflection are found to be governed by the fractional parts of the average thickness of the layer (in monolayers). We conclude that each structure has two scales of fluctuations which form the relief of the AlAs surface. The largest fluctuations repeat the relief of the GaAs surface. The second scale has the size of a typical XΓ exciton Bohr radius. The smaller fluctuations disappear when the thickness of the AlAs layer is equal to an integer number of monolayers, which provide interfaces of the quality. The correlation of macro-rough fluctuations on the surface of AlAs and GaAs causes an asymmetry in the densities of states of type II excitons located at either AlAs-on-GaAs or GaAs-on-AlAs interfaces. Hence the lowest PL line is formed by excitons localized across the AlAs-on-GaAs interface. On the other hand, in structures with micro-rough but uncorrelated AlAs surfaces, the lowest energy state is expected to be occupied by excitons localized across the GaAs-on-AlAs interface.

scholarly journals The reaction between type II pneumococcus antiserum and a glucuronide azo-protein

1941 ◽  
Vol 130 (858) ◽  
pp. 60-69 ◽  
Keyword(s):  
Glucuronic Acid ◽  
Amino Derivative ◽  
Type Ii ◽  
Animal Protection ◽  
Specific Polysaccharide ◽  
Serum Ratio

An amino derivative of the natural glucuronide, euxanthic acid, was prepared and coupled by the azo-link to proteins. These azo-proteins gave precipitates with type II pneumococcus antiserum, which were inhibited by glucuronides. The effect of varying azoprotein/serum ratio on the amount and com position of the precipitate was similar to the effect of varying polysaccharide/serum ratio on the precipitate form ed when the specific polysaccharide is added to the serum. Attempts to immunize rabbits and mice with a ino-euxanthic acid azoprotein were not successful. Chemical estimations and animal protection experiments indicated that the material precipitated by the azo-protein from the serum was part of the antibody to type II pneumococcus. These results support the view that at any rate part of the specificity of type II serum for the type polysaccharide is due to glucuronic acid or some closely similar grouping.

scholarly journals Occurrence of West Nile Virus Antibodies in Wild Birds, Horses, and Humans in Poland

2015 ◽  
Vol 2015 ◽  
pp. 1-5 ◽  
Author(s):  
Jowita Samanta Niczyporuk ◽  
Elżbieta Samorek-Salamonowicz ◽  
Sylvie Lecollinet ◽  
Sławomir Andrzej Pancewicz ◽  
Wojciech Kozdruń ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Japanese Encephalitis ◽  
Wild Bird ◽  
Horse Serum ◽  
Wild Birds ◽  
Serum Samples ◽  
West Nile ◽  
Cross Reactions ◽  
Lymphocytic Meningitis ◽  
Positive Results

Serum samples of 474 wild birds, 378 horses, and 42 humans with meningitis and lymphocytic meningitis were collected between 2010 and 2014 from different areas of Poland. West Nile virus (WNV) antibodies were detected using competition enzyme linked immunosorbent assays: ELISA-1 ID Screen West Nile Competition, IDvet, ELISA-2 ID Screen West Nile IgM Capture, and ELISA-3 Ingezim West Nile Compac. The antibodies were found in 63 (13.29%) out of 474 wild bird serum samples and in one (0.26%) out of 378 horse serum samples. Fourteen (33.33%) out of 42 sera from patients were positive against WNV antigen and one serum was doubtful. Positive samples obtained in birds were next retested with virus microneutralisation test to confirm positive results and cross-reactions with other antigens of the Japanese encephalitis complex. We suspect that positive serological results in humans, birds, and horses indicate that WNV can be somehow closely related with the ecosystem in Poland.

scholarly journals SPECIFIC ANTIBODY RESPONSE OF HUMAN SUBJECTS TO INTRACUTANEOUS INJECTION OF PNEUMOCOCCUS PRODUCTS

1932 ◽  
Vol 55 (6) ◽  
pp. 853-865 ◽  
Author(s):  
Maxwell Finland ◽  
W. D. Sutliff
Keyword(s):  
Human Subjects ◽  
Type I ◽  
Type Ii ◽  
Specific Antibody Response ◽  
Specific Antibodies ◽  
Virulent Strains ◽  
Before And After ◽  
Specific Polysaccharide ◽  
Protective Antibodies ◽  
Intracutaneous Injection

The blood of 63 human subjects selected because of the absence of recent infections, was studied for its content of specific antibodies against virulent strains of Types I, II, and III pneumococci before and after intracutaneous injections of minute amounts of pneumococcus products. The simultaneous injection of the specific polysaccharides of all three types of pneumococci and of proteins and autolysates derived from Types I and II pneumococci was followed by the appearance or increase of pneumococcidal power in the whole defibrinated blood and, in most instances, by the appearance of mouse-protective antibodies and agglutinins for one or more types. A single intracutaneous injection of 0.01 mg. of the protein-free type-specific polysaccharide of either Type I, Type II, or Type III pneumococci or 4 similar daily injections was followed, in most of 29 subjects, by the appearance of antibodies against the homologous, but not against the heterologous type pneumococci. Some subjects showed a simultaneous lowering of a preexisting pneumococcidal power for heterologous or homologous types. A single intracutaneous injection of O.1 mg. of pneumococcus protein in 13 individuals was not followed by the appearance of specific antibodies to any appreciable degree. Single intracutaneous injections of small amounts of autolysates derived from virulent strains of Type I, II, or III pneumococci were followed in 11 subjects by a more or less general rise in the pneumococcidal power with the appearance of homologous type agglutinins and protective antibodies in about one-third of the subjects.

scholarly journals CHEMO-IMMUNOLOGICAL STUDIES ON CONJUGATED CARBOHYDRATE-PROTEINS

1937 ◽  
Vol 66 (2) ◽  
pp. 191-205 ◽  
Author(s):  
Walther F. Goebel ◽  
Rollin D. Hotchkiss
Keyword(s):  
Carboxylic Acids ◽  
Galacturonic Acid ◽  
Horse Serum ◽  
Type I ◽  
Specific Antibodies ◽  
Cross Reactions ◽  
Normal Horse Serum ◽  
High Dilutions ◽  
Serum Type

1. Azoprotein antigens containing glucuronic and galacturonic acids give rise in rabbits to specific antibodies. The immune sera show no serological crossing with antigens containing glucose or galactose. 2. The galacturonic acid antigen reacts in antipneumococcus horse serum Type I in high dilutions. 3. Azoprotein antigens containing galacturonic acid, benzene sulfonic and carboxylic acids precipitate in antipneumococcus horse sera of various types but not in normal horse serum. The mechanism underlying these cross reactions is discussed.

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