scholarly journals A STUDY OF THE EFFECT OF SERUM ON THE IMMUNOLOGICAL REACTION OF A BACTERIAL ENDOTOXIN

1956 ◽  
Vol 103 (4) ◽  
pp. 439-452 ◽  
Author(s):  
Leighton E. Cluff
Keyword(s):  
Human Serum ◽  
Serratia Marcescens ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Immunological Reaction ◽  
Beta Globulin ◽  
Zone Electrophoresis ◽  
Polysaccharide Antigens ◽  
Relationship Of

Contact of a purified endotoxin from Shigella fiexneri Type Z with normal rabbit or human serum results in an alteration of its immunological reaction with antiserum, as determined by precipitation in gel. Analysis of fractions of normal serum obtained by zone electrophoresis in starch indicates that the component responsible for altering the immunological reaction of endotoxin is associated with beta globulin. Normal serum has no similar effect on the immunological reaction of a variety of other protein and polysaccharide antigens. Serum from rabbits made tolerant to the pyrogenic action of an endotoxin from Serratia marcescens (P-35) possesses the ability to alter the reaction of Shigella endotoxin with its specific antiserum, although the serum from tolerant rabbits does not significantly enhance the pyrogenicity of Shigella toxm. The component of normal rabbit serum responsible for the effect on the immunological reaction of Shigella endotoxin is not destroyed by heating at 56°C. The possible relationship of the effect of normal serum on the immunological reaction of endotoxin and the augmentation of fever induced by endotoxins 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.

Lipid transport and lipoprotein interconversions

1961 ◽  
Vol 200 (6) ◽  
pp. 1307-1310 ◽  
Author(s):  
Scott M. Grundy ◽  
Harold L. Dobson ◽  
George E. Kitzmiller ◽  
A. Clark Griffin
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Lipid Transport ◽  
Rabbit Serum ◽  
Analytical Ultracentrifuge ◽  
Serum Lipoproteins ◽  
Phospholipid Complex ◽  
Beta Globulin ◽  
Cold Ether ◽  
Preparative Ultracentrifugation

Serum lipoproteins were isolated from various sources including normal and hyperlipemic human, dog, and rabbit serum through preparative ultracentrifugation. These lipoprotein fractions were extracted with cold ether, and the ether-modified products were studied for sedimentation and flotation properties in an analytical ultracentrifuge. Results indicate that a relatively small number of ether-modified residues are obtained from the entire lipoprotein spectrum of all species studied. It is suggested that these moieties may be closely related to actual lipid-transporting components of the lipoprotein system. In addition, a fraction of lipoprotein-free human serum (probably closely related to beta globulin) has been identified, which will bind certain phospholipids. This protein-phospholipid complex may be separated from other serum proteins through ultracentrifugation and studied electrophoretically.

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.

Nonadrenergic noncholinergic neurotransmitter of feline trachealis: VIP or nitric oxide?

1993 ◽  
Vol 74 (1) ◽  
pp. 31-39 ◽  
Author(s):  
J. T. Fisher ◽  
J. W. Anderson ◽  
M. A. Waldron
Keyword(s):  
Nitric Oxide ◽  
Muscle Tone ◽  
Passive Immunization ◽  
Electrical Field Stimulation ◽  
Isometric Tension ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Response Curves

We tested the hypothesis that vasoactive intestinal peptide (VIP) or nitric oxide (NO) is the nonadrenergic noncholinergic (NANC) neurotransmitter in feline trachealis. Isometric tension was measured in trachealis (open or closed tracheal rings) in vitro. Propranolol (10 microM) and atropine (1 microM) were present throughout the experiment, and smooth muscle tone was increased to 60–90% maximal with 5-hydroxytryptamine. We used three methodologies to reduce the relaxation function of VIP, which in turn should reduce NANC-mediated relaxation. 1) The putative VIP antagonist peptide T (10 microM) did not affect VIP concentration-response curves or electrical field stimulation- (EFS) induced NANC responses. 2) Incubation of tissue in specific VIP antiserum (16 h at 4 degrees C) did not reduce EFS-induced NANC relaxations relative to tissue incubated in normal rabbit serum (P > 0.05). On the basis of our passive immunization techniques, it is not possible to absolutely reject VIP as the NANC transmitter. We speculate that nonspecific peptidases present in normal serum and VIP antiserum reduce EFS-induced responses similarly. 3) VIP desensitization, confirmed by a significant rightward shift (P < 0.01) in the VIP concentration-response curve, was achieved by exposing tissues (n = 11) to 1.0 microM VIP for 30 min. Desensitization did not reduce the EFS-induced NANC relaxatory response (P < 0.05) compared with control tissues, suggesting that VIP is not the NANC mediator.(ABSTRACT TRUNCATED AT 250 WORDS)

THYROGLOBULIN IMMUNITY

1968 ◽  
Vol 59 (1) ◽  
pp. 159-171 ◽  
Author(s):  
A. K. Medda ◽  
B. N. Premachandra
Keyword(s):  
Immune Globulin ◽  
Binding Sites ◽  
Hind Limb ◽  
Rana Catesbeiana ◽  
Potent Inhibitor ◽  
Protein Complexes ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
The Media

ABSTRACT Metamorphosis of Rana catesbeiana tadpoles immersed in a medium containing thyroxine (T4) occurred in 58 days, whereas 79 days were required for tadpoles treated with albumin + T4 complex in media, and at 121 days 50 % metamorphosis occurred in the group whose medium contained normal rabbit serum + T4. No metamorphosis occurred in tadpoles which had rabbit antiporcine thyroglobulin + T4 complex in media. Similarly the retardation of hind limb growth in comparison to the control at 58 days was most severe in animals treated with antithyroglobulin + T4 complex in media (74.3 % depression) followed by normal serum + T4 (60.1 % less) and bovine albumin + T4 complex (30 % inhibition) treated animals. In further investigations, in comparison to controls (only 125I-T4 in media), 62.4%, 77.0%, and 82.4% less 125I-T4 concentration was seen in viscera, tail, and carcass respectively of tadpoles treated with immune globulin + 125I-T4 in the media, whereas no change was seen in the group treated with normal gammaglobulin + 125I-T4 complex; similarly no changes in visceral 125I-T4 concentration were noted in groups whose media contained thyroglobulin in complex with 125I-T4. Present investigations therefore show that normal rabbit serum (apparently any good T4 binding protein) is a potent inhibitor of metamorphosis of tadpoles, the effectiveness mediated at least in part, on the inability of the larva to split thyroxine-protein complexes in their body. Antiporcine thyroglobulin rabbit serum was shown to be superior to normal rabbit serum in inhibiting tadpole metamorphosis, evidently due to additional T4 binding sites provided by the immune globulin. Available evidence indicates that antithyroglobulin binding of T4 is distinct and is evidently not due to thyroglobulin that may be in complex with the thyroid antibody.

scholarly journals THE EFFECT OF TESTICLE EXTRACT AND OF NORMAL SERUM ON A TRANSPLANTABLE EPITHELIAL TUMOR OF THE RABBIT

1931 ◽  
Vol 54 (4) ◽  
pp. 493-498 ◽  
Author(s):  
F. Duran-Reynals
Keyword(s):  
Tumor Cell ◽  
Cell Suspension ◽  
Pathogenic Bacteria ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Epithelial Tumor ◽  
Tumor Cell Suspension

Extract of rat, rabbit or bull testicle prevents or retards the growth of a rabbit tumor when a mixture of the extract and a tumor cell suspension is inoculated intradermally. Similar mixtures, made with normal rabbit serum instead of testicle extract, give rise to tumors which grow with unusual rapidity. The results are the opposite of those obtained with pathogenic bacteria or filtrable viruses which are enhanced by testicle extract and generally inhibited by normal serum.

scholarly journals A Study of Non-specific Complement-fixation with particular reference to the Interaction of Normal Serum and certain Non-antigenic substances

1928 ◽  
Vol 28 (2) ◽  
pp. 172-197 ◽  
Author(s):  
T. J. Mackie ◽  
M. H. Finkelstein
Keyword(s):  
Human Serum ◽  
Complement Fixation Test ◽  
Complement Fixation ◽  
Normal Serum ◽  
Fixation Test ◽  
Normal Human Serum ◽  
Rabbit Serum ◽  
Considerable Proportion ◽  
Normal Human ◽  
Fixation Reaction

1. When a solution of commercial peptone is substituted for antigen in a complement-fixation test with the unheated normal serum of certain species (man, ox, sheep, horse, rabbit, white rat), a definite fixation reaction occurs both at 37° C. and at 0° C. In the ox, sheep, horse and rabbit this property of serum is partially stable at 55° C., but normal human serum and the serum of the white rat are inactive after heating at this temperature. The property is resident mainly in the carbonic-acid-insoluble globulins of the serum.2. The same results are obtained when ethyl alcohol diluted with several volumes of normal saline solution is substituted for antigen in a complement-fixation test with normal serum.3. Analysis of these reactions shows a close correspondence with complement-fixation by the sera of normal animals plus the Wassermann “antigen”—the Wassermann reaction of normal animals.4. Marked complement-fixation effects are also obtained with heated normal serum of the rabbit, ox, sheep, horse plus cholesterol suspension, and particularly cholesterolised-peptone, these effects occurring in parallel with those produced by serum plus alcohol-saline, peptone solutions and the Wassermann “antigen.” The heated normal serum of the pig, white rat and guinea-pig do not exhibit these reactions, and the same applies to heated normal human serum. Unheated pig serum fails to react. Such results also elicit a close relationship between these non-specific reactions and the Wassermann reactions of normal animals.5. The reacting property is absent from the serum (heated and unheated) of young rabbits during the first 2 to 3 weeks of life, but appears soon after this (e.g. by the 37th day) and is progressive in development. Its development in early life runs parallel to that of the natural haemolytic property of the serum for sheep's blood (due to a natural antibody-like substance). The two properties are, however, independent as illustrated by absorption tests.6. Besides the agents referred to above as capable of fixing complement along with normal sera, other substances possess a similar property, e.g. certain alcohols, sodium oleate, tissue proteins, certain amino-acids and sodium nucleate. Commercial peptone purified by precipitation with alcohol is equally active with the original material. Cholesterolisation of these agents may yield a product whose activity is greater than that due to summation of effects.7. Wassermann-positive and -negative human sera have been tested in the complement-fixation reaction with certain of these “pseudo-antigens,” viz. alcohol-saline, peptone, cholesterol, and cholesterolised-peptone, but a uniform parallelism has not been demonstrated between the reactions with these agents and the Wassermann effect. Some Wassermann-positive sera react also with alcohol-saline, peptone, cholesterol and cholesterolised-peptone, while sera from selected normal persons are quite inactive. A considerable proportion of Wassermann-positive sera yields definite complement-fixation with cholesterol and cholesterolised-peptone; a small proportion of Wassermann-negative sera reacts with these agents.8. The thermolability of the serum principles acting with various “pseudoantigens” has been studied by testing unheated serum and serum heated at temperatures ranging from 46° to 60° C. Two types of thermolability curve have been demonstrated with different specimens of rabbit serum: (1) a more or less progressive weakening of the various reactions with inactivation at 60° C.; (2) inactivation of the effects with Wassermann “antigen,” alcoholsaline and cholesterol at 50–52° C., activation of the effects with the Wassermann “antigen” and cholesterol at 54–56°C. and inactivation again above 60° C.; in this case the curves for peptone and cholesterolised-peptone do not show such double inactivation. Unheated normal human serum yields reactions with the various agents (including the Wassermann “antigen”) but inactivation occurs at 50° to 54° C. whereas certain syphilitic sera yield thermolability curves somewhat similar to type (1) of rabbit serum, with inactivation at 60° C. or over.

scholarly journals THE INTERACTION IN VITRO BETWEEN GROUP B MENINGOCOCCI AND RABBIT POLYMORPHONUCLEAR LEUKOCYTES

1967 ◽  
Vol 126 (5) ◽  
pp. 795-818 ◽  
Author(s):  
Richard B. Roberts
Keyword(s):  
Bactericidal Activity ◽  
Polymorphonuclear Leukocytes ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Opsonic Activity ◽  
Heat Stable ◽  
Group B

The interaction in vitro between group B meningococci and rabbit polymorphonuclear leukocytes has been described. Phagocytosis did not occur in the presence of normal rabbit serum. Antiserum collected 12–21 days following one subcutaneous inoculation of living log phase meningococci exhibited opsonic activity with type specificity; this opsonic action depended on both heat-labile and heat-stable factors. Following ingestion by granulocytes, meningococci were rapidly killed. These studies suggest that group B meningococcal strains contain specific antiphagocytic surface factors of an as yet unknown chemical nature. Antisera obtained 4 or more wk after immunization showed bactericidal activity with the same type specificity as opsonic activity. This bactericidal activity was also lost after heating and restored by the addition of normal serum. Further studies on opsonins and bactericidins for meningococci may shed light on virulence factors in these microorganisms, and may prove useful for a more precise classification of meningococci according to type rather than group specificity.

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