Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PRECIPITINS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,135 records · Page 63Linked to original sources
PubMed1991

Prevalence of serum precipitating antibodies in horses to fungal and thermophilic actinomycete antigens: effects of environmental challenge.

Sera from 54 two- to three-year-old Thoroughbred horses from an English racing stable were examined for precipitins to antigen extracts prepared from 18 species of moulds (fungi and thermophilic actinomycetes) isolated from the same stable. Twenty-seven horses exhibited serum precipitins to one or more antigens; sixteen of the mould antigens elicited positive reactions in sera from one or more horses. Significantly more precipitins occurred in sera of those horses stabled in a barn than among those stabled in individual boxes. This indicated a possible association between type of housing, level of exposure to airborne moulds and presence of serum precipitins. None of the horses had overt respiratory disease. This study agrees with reports of the presence of serum precipitating antibodies to mould antigens in clinically healthy horses and confirms that serological tests, therefore, are of little value in the diagnosis of chronic obstructive pulmonary disease (COPD) or 'heaves'.

Actinomycetales↗
PubMed1970

Relationship between staphylococcal antiserum titer and zone development on immune serum plates.

A workable relationship was established between the standard serum titers of staphylococcal immune antisera and the development of precipitin zones on serum agar around colonies of staphylococcal strains producing homologous antigens (enterotoxins). The standard titer of a serum is defined as the reciprocal of that serum dilution which, with 10 mug of pure enterotoxin per ml, will give a precipitin zone 10 mm in length in single gel-diffusion tubes after 7 days of incubation at 25 C. A numerical scale was set up for determining the intensity of precipitin zones on serum agar. A reading of 3 was considered optimum. This correlated well with a standard serum titer of 25, when 1 ml of such a serum was used per 20 ml of medium per serum plate. From this relationship, the minimum volume of serum required to give optimum precipitin zone development can be calculated.

Agar↗
PubMed1973

Detection and identification of diagnostic Histoplasma capsulatum precipitates by counterelectrophoresis.

Studies were carried out to develop and evaluate a counterelectrophoresis (CEP) technique for the rapid and specific identification of the diagnostically important histoplasmosis H and M precipitin bands. Well-defined and centrally located precipitin bands were produced by using a discontinuous buffer system and a gel matrix composed of agarose and ionagar no. 2. A template was devised which allowed the selective identification of the H and M precipitins. Comparative evaluations were performed with the microimmunodiffusion (ID) and complement fixation tests. In 52 sera from persons with histoplasmosis, either the H or M precipitin, or both, were identified in 42 (81%) of the cases with the CEP technique and in 43 (83%) with the ID test. With sera from 28 persons with heterologous diseases, the CEP technique, like the ID test, failed to react. The specificity of the CEP technique was dependent upon the use of the identity template. The CEP technique is recommended for routine use in laboratories testing moderate numbers of sera. It provides accurate and reproducible results within 90 min, in contrast to the ID test, which requires 18 to 24 h.

Antibodies, Fungal↗
PubMed1978

Filamentous capsulated streptococci from the human respiratory tract: chemical and immunochemical characterization of a glycoprotein capsular antigen of provisional binary capsular type 87.

A filamentous alpha-hemolytic streptococcus of provisional capsular type 87 isolated from the human respiratory tract has been shown to be binary capsulated. One of the capsular antigens appears to be a glycoprotein; the other appears to be a polysaccharide. Transformation reactions with deoxyribonucleic acid from streptococcus type 87 and a number of noncapsulated pneumococci yielded transformed pneumococci with either a glycoprotein capsule or a polysaccharide capsule, but not with both. Capsular precipitin (quellung) reactions were observed when streptococcus type 87 was treated with homologous antiserum or with antisera to either of the two distinct capsular transformants. Each of the transformed pneumococci gave a quellung reaction with its homologous antiserum or with antiserum to streptococcus type 87, but neither reacted with antiserum to the heterologous transformant. Chemical analysis showed the glycoprotein antigen of streptococcus type 87 to contain, in addition to amino acids, glucose, galactose, glucosamine, and phosphate. The amino acid composition of the glycoprotein capsular antigens from streptococcus type 87 and of those from transformed pneumococci were similar, showing only minor differences. The glycoprotein capsular antigen from streptococcus type 87 gave two closely associated precipitin bands with homologous antiserum or antisera to transformed pneumococci with the glycoprotein capsule. That the two precipitin bands represent two unrelated proteins is precluded largely on the basis of the unlikely probability of 100% cotransformation of the genes coding for both proteins in the pneumococcal transformants that were isolated. Chemical analyses of the various fractions of the glycoprotein indicate that the two precipitin bands may represent a glycoprotein and its corresponding apoprotein.

Amino Acids↗
PubMed1982

Hemagglutination activity and colonization factor antigens I and II in enterotoxigenic and non-enterotoxigenic strains of Escherichia coli isolated from humans.

We examined 205 enterotoxigenic strains of Escherichia coli for colonization factor antigens (CFA) I and II, using an immunodiffusion technique with specific antisera. A total of 36 strains of serogroups O63, O78, O114, O128, and O153 and 1 rough strain possessed CFA/I and gave a single precipitin line; 47 strains of serogroups O6, O8, O80, and O115 possessed CFA/II. The latter strains gave a major precipitin line (component 3) when tested with specific antisera prepared against strain E1392 or PB-176 (both E. coli O6.H16; biotype A). However, all 16 strains of E. coli O6.H16 belonging to biotype A gave a second precipitin line (component 1) when tested with both antisera. When CFA/II-positive strains were tested with a specific antiserum prepared against E. coli O6.H16 strains of biotype B or C, all strains gave component 3, but 16 of 17 strains of E. coli O6.H16 belonging to biotype B, C, or F gave a second precipitin line (component 2) not given by strains of biotype A. CFA/II-positive strains of serogroups other than O6 gave only component 3 in tests with all specific antisera. Nine enterotoxigenic strains of serotypes O7, O15, O25, O115, and O128 gave mannose-resistant hemagglutination of human or calf erythrocytes but lacked CFA/I or CFA/II. Although mannose-resistant hemagglutination was common in non-enterotoxigenic strains of E. coli, none of the non-enterotoxigenic strains possessed CFA/I or CFA/II; these strains included fecal strains of serogroups O6, O8, O63, and O78, fecal strains of enteropathogenic serogroups, and strains from extraintestinal sources.

Animals↗
PubMed1968

Comparative studies of antigens from Mycoplasma mycoides and Escherichia coli.

Extracts of sonically disrupted Mycoplasma mycoides and Escherichia coli were fractionated by sucrose density gradient centrifugation. The presence of antigen in each of the fractions was determined by complement-fixation and agar-gel diffusion precipitin tests, in which cow, pig, and rabbit anti-M. mycoides sera and rabbit anti-E. coli serum were used. Fractions of M. mycoides, with a buoyant density of 1.225 or lower, fixed complement with cow and pig anti-M. mycoides sera. These fractions also formed precipitin lines with pig antiserum. Fractions in the buoyant density range of 1.10 to 1.20 fixed complement with rabbit anti-E. coli serum, but precipitin lines were not formed. All E. coli fractions fixed complement and gave precipitin lines with homologous serum. But fractions in the buoyant density range of 1.10 to 1.20 had minimal complement fixation with heterologous M. mycoides sera. The cross-reacting antigens in M. mycoides and E. coli had a buoyant density of 1.10 to 1.20; the specific antigens were isolated from M. mycoides at a buoyant density of 1.08 to 1.02.

Animals↗
PubMed1986

Immunodiffusion test for diagnosing and monitoring pythiosis in horses.

A practical, sensitive, and specific immunodiffusion test was developed for diagnosing and monitoring pythiosis in horses. Culture filtrates, a soluble cell mass, and trypsinized Pythium sp. antigens were evaluated against prepared rabbit anti-Pythium sp. serum and pythiosis horse case sera. The culture filtrate antigens demonstrated the greatest capacity for detecting precipitins and the greatest stability during storage. In contrast, the trypsinized antigens had the weakest capability for detecting multiple precipitins and the poorest stability. The 13 sera from horses with proven active pythiosis were positive in immunodiffusion tests with the culture filtrate antigens. Each serum contained from three to six precipitins. Treated horses lost precipitins, and some became antibody negative. No false-positive reactions were noted in tests with sera from normal horses and humans or with sera from a variety of heterologous horse and human infections.

Animals↗
PubMed1982

Aspergillus terreus, a pathogen capable of causing infective endocarditis, Pulmonary mycetoma, and allergic bronchopulmonary aspergillosis.

Aspergillus terreus is a rarely reported pathogen in humans, Recovery of this organism from the sputum may therefore be discounted as representing contamination this report describes 3 patients--1 with allergic bronchopulmonary aspergillosis (ABPA), 1 with aspergilloma, and 1 with infective endocarditis-- in whom A. terreus was proved to be the etiologic organism. Together, these 3 cases span the spectrum of disease usually associated with A. fumigatus. Detection of serum precipitins against Aspergillus is essential to a diagnosis of both ABPA and aspergilloma. In our 2 patients with these syndromes, serum precipitins were specific for A. terreus ane did not cross-react with A. fumigatus or mixed Aspergillus antigens. This finding suggests that screening of serum for precipitins were specific for A. terreus and did not cross-react with A. fumigatus or mixed Aspergillus antigens. This finding suggests that screening of serum for precipitins should be carried out with A. terreus antigen in patients suspected of harboring this organism.

Adolescent↗
PubMed2000

A prospective study of nasal disease in adult cystic fibrosis.

Twenty-six adult cystic fibrosis patients were studied to compare nasal disease with their laboratory correlates including skin testing, immunoglobulin and Aspergillus fumigatus precipitin levels, saccharin testing and sputum cultures. Six patients were asymptomatic and all of these had negative skin tests, normal IgE levels and negative Aspergillus fumigatus precipitins. Thirteen patients had rhinitis, 12 had positive skin-testing for common allergens, 10 elevated IgE levels and nine positive Aspergillus fumigatus precipitins. Seven patients had polyps, all had normal IgE levels and negative Aspergillus fumigatus precipitins, six had positive skin testing for common allergens. There also appeared to be a relationship between Pseudomonas spp. colonization and positive skin testing.

Adolescent↗
PubMed1985

Determination by enzyme-linked immunosorbent assay (ELISA) of specific IgG antibody activities for diagnosis of farmer's lung disease.

The specific IgG antibodies to thermophilic actinomycetes in the sera from patients with farmer's lung disease were quantitated by an ELISA and the results thereof were compared with those obtained by the standard double immunodiffusion assay (Ouchterlony's method). All sera from patients with farmer's lung disease were precipitin positive to Thermoactinomyces vulgaris and/or Micropolyspora faeni by the Ouchterlony's method, and revealed significantly high levels of IgG antibody activities against these antigens by ELISA. We have found 18 precipitin-positive but asymptomatic subjects in a survey of the dairy farming population of the northern area of IWATE Prefecture. Their sera were precipitin positive to antigens related to the farmer's lung disease, however IgG antibody activities as determined by ELISA to these antigens was significantly lower in the group of asymptomatics than in the group of symptomatics. Precipitin negative dairy farming controls and normal controls living in the urban area revealed low antibody activities as determined by ELISA. From these studies, we concluded that the assay of specific IgG antibody activity to thermophilic actinomyces by ELISA is useful for the diagnosis and screening of farmer's lung disease.

Adult↗
PubMed1982

Immunological properties of erythrocyte catalase in Japanese type acatalasemia.

The reaction between acatalasemia hemolysate and anti-normal erythrocyte catalase IgG gave a precipitin line which was interrupted by a normal precipitin line, in the double immunodiffusion method. Hypocatalasemia hemolysate revealed two precipitin lines, one completely, the other partially, fused with a normal precipitin line. No immunological reactions between fresh hemolysates of acatalasemia, hypocatalasemia and normal erythrocytes and antihuman C-reactive protein serum were observed, but the lysates stored for 4 weeks in an ice cold water bath reacted slightly with this antiserum.

Catalase↗
PubMed1980

Antibodies to proteins from yolk of immunized hens.

Immunoglobulins IgY, extracted from yolks of hens immunized against several proteins and natural mixtures of proteins were examined by the Ouchterloney gel diffusion and Laurell immuno-electrophoresis techniques. The molecular weights of the proteins ranged from 8 x 10(6) to less than 2 x 10(4). The hens produced IgY antibodies readily when injected with the high molecular antigens > 150 000 but did not react as well to antigens of relatively low molecular weight < 30 000. Optimal precipitin reactions were obtained with low molecular antigens when the agarose gel contained 1.5 M NaCl. Salt concentration (0.15-1.5 M NaCl) has no effect on the precipitin reaction in gels on the systems of high molecular antigens and their IgY antibodies apart from a displacement of the precipitin line. From the relative positions of the precipitin lines to the wells containing the reactants it would appear that the IgY formed dimers when the concentration of NaCl is 1.6 M and remain as monomers in gels containing 0.15 M NaCl. An explanation of the salt effect is offered.

Amoeba↗
PubMed1979

[Immunoelectrophoresis for Fasciola hepatica]

In an attempt to investigate the specific antigenic substance of Fasciola hepatica, Ouchterlony tests and immunoelectrophoretic analyses were carried out. Crude Fasciola antigen was prepared and fractionated by Sephadex G-200 column to Antigen I, II and III according to protein content. Crude antigens of Paragonimus westermani, Clonorchis sinensis and Paramphistomum sp. were also prepared for control and absorption study. Antiserum was prepared by injecting 0.5 ml of crude Fasciola antigen with same amount of complete Freund's adjuvant in rabbits, 10 times at an interval of l week. The results obtained in this study were as follows: 1. Crude Fasciola antigen reacted with antiserum with 9 precipitin bands by Ouchterlony test and with 11 bands by immunoelectrophoresis. 2. Cross reaction was observed between Paragonimus, Clonorchis and Paramphistomum antigens and anti-Fasciola rabbit serum respectively. By Ouchterlony test, 3-4 cross reacting bands were found. 3. Anti-Fasciola sera which were absorbed with respective Paragonimus, Clonorchis and Paramphistomum antigens, reacted with Fasciola crude antigen. Ouchterlony test gave 5-6 precipitin bands. Further reaction between Fasciola antigen and antiserum absorbed with the above 3 antigens concomitantly gave 5 precipitin bands by Ouchterlony test and 7 bands by immunoelectrophoretic analyses. 4. Fractionated Fasciola antigens (Antigens I, II & III) reacted with anti-Fasciola rabbit serum in immunoelectrophoresis. Antigen I, II and III gave 2, 3 and 5 precipitin bands respectively. Anti-Fasciola rabbit serum which was absorbed with 3 trematodes antigens gave, by immunoelectrophoresis, 1 band with Antigen I, 2 bands with Antigen II and III of Fasciola hepatica. From the above results, it is concluded that Fasciola hepatica possessed the specific antigenic substance not cross-reacted with other trematodes.

Journal Article↗
PubMed1985

Assays for Sm and RNP antibodies: pitfalls and technical considerations.

Sm antibodies are a specific serum marker for the diagnosis of systemic lupus erythematosus (SLE), and a high titer of RNP antibodies in the absence of other antinuclear antibodies (ANA) is highly suggestive of the diagnosis of mixed connective tissue disease (MCTD); therefore, specificity is a very important aspect of the assays for these antibodies. Currently in the clinical laboratory, double immunodiffusion (ID) is the most specific of the assays for anti-Sm and RNP. When 74 sera from patients with various systemic rheumatic diseases were assayed by counterimmunoelectrophoresis (CIE) with ID as the reference method, three sera contained nonspecific (non-Sm) precipitin lines in the assay for anti-Sm and three sera contained nonspecific (non-RNP) precipitin lines in the assay for RNP. Precipitin lines formed by the common antinuclear antibodies are more clearly separated by ID than CIE and care must be taken to avoid false identification of precipitin lines with CIE. Indirect immunofluorescence is recommended for ANA screening, ID for definitive antibody identification, and CIE for antibody quantification.

Antibodies, Antinuclear↗
PubMed1981

The application of immunodiffusion test to the estimation of hydrolysis of mycobacteria proteins by proteolytic enzymes of mice peritoneal cells.

The possibility of applying the immunodiffusion (ID) test in agarose gel to detect the degradation of the somatic proteins of mycobacteria BCG-Poland by proteolytic enzymes of non activated and activated mice peritoneal cells was investigated. Degradation of those proteins was determined by disappearance of some precipitin lines resulting from the hydrolysis. The immunodiffusion test was found to be useful to show the degradation of protein of mycobacteria by cathepsins of mice peritoneal cells. Disappearance of 4 precipitin lines in ID test occurred after 3 h incubation of mycobacteria proteins with extracts of non activated mice peritoneal cells at pH 3, which gives evidence of degradation of some mycobacteria antigens. The extention of the time of incubation up to 24 h gave the same results. At the incubation at pH 4.5 no disappearance of precipitin lines was observed. It was found that cathepsins no specifically activated mice peritoneal cells degradate mycobacteria proteins at pH 3 and pH 4.5. Degradation occurred more rapidly at pH 3 achieving maximal effect after 6 h. The degree of degradation at pH 4.5 increased during the whole period of examination, i.e. up to 24 h of incubation time after which a disappearance of 5 precipitin lines was found. No degradation was found after incubation at pH 6 and pH 8.

Acid Phosphatase↗
PubMed1984

Problems in the serodiagnosis of canine brucellosis: dog responses to cell wall and internal antigens of Brucella canis.

Three procedures are commonly used for the serodiagnosis of B. canis infection: 1) The rapid slide agglutination test (RSAT), 2) the tube agglutination test (TAT), and 3) the modified 2-mercaptoethanol tube agglutination test (2ME-TAT). Hemocultures are always essential for diagnosis. The RSAT was developed to provide a presumptive diagnosis rapidly. It has been found accurate in identifying non-infected dogs; however false positive reactions are common due to shared determinants between the surface antigens of B. canis and certain other gram-negative bacteria. The RSAT has recently been modified to include brief reaction of test sera with 2ME (0.2M) prior to adding test antigen. The modification has improved specificity, but it has not eliminated false positive reactions. The TAT and 2ME-TAT are widely used. Although there is good agreement between tests, both suffer from lack of specificity but are valuable in kennels where B. canis has been identified by blood cultures. Agarose gel immunodiffusion (AGID) tests using extracted (SDC or hot PBS) cell wall antigenic complexes reveal precipitins in the sera of infected dogs usually 8 to 12 weeks postinfection (PI) that may persist 5 years. The antigenic complexes consist of at least 3 antigens; one (antigen '2R') appears to possess high B. canis specificity. Sera from noninfected dogs also may react nonspecifically in AGID tests that employ crude SDC or PBS antigenic extracts leading to 'false positive' interpretations. Cytoplasmic antigens gave up to four precipitin lines with sera from B. canis infected dogs. The antigens (protein or glycoprotein) were present in both S and R Brucella cells, but not in other gram-negative organisms examined. AGID tests that employed cytoplasmic antigens revealed precipitins against one or more (usually 2-3) antigens from PI months 4 through 64. In some dogs, precipitins were present 12 months after the bacteremia had ceased, a time when other tests were diagnostically insignificant, or equivocal. No 'false positive' field sera reached with the cytoplasmic antigens.

Animals↗
PubMed1981

Development and characterization of feline ovarian antiserum.

Studies were conducted to determine the feasibility of producing feline ovarian antiserum (FOA) in the rabbit and to characterize the antigenic composition of the feline ovary. Adult male rabbits were immunized by injecting an ovarian homogenate prepared from feline ovaries that had corpora lutea (CL) macroscopically removed. Using the agar-gel double diffusion (AGDD) and the immunoelectrophoretic (IE) techniques, 5 feline ovarian antigens were detected when feline ovarian extract was reacted with purified FOA (gamma-globulin fraction solution; protein content 24 mg/ml). The FOA reacted with 4 other feline reproductive organs tested, including the follicle, CL, oviduct, and uterus, to form 5 precipitin bands. The purified FOA also cross-reacted with feline serum and plasma and 10 other feline nonreproductive organ extracts tested to give 2 to 5 precipitin bands. Species cross-reactivity was also observed with FOA reacting with the rat ovary and the canine ovary, CL, and uterus, to form 1 to 2 precipitin bands. Immunoabsorption of the purified FOA by feline fever, kidney, or small intestine extract removed antibodies reacting with feline ovarian antigens. Precipitin bands failed to develop when such absorbed FOA were tested against the feline ovarian extract. Within the sensitivity limits of the AGDD and IE tests, organ-specific antigens of the feline ovary could not be detected. Feline ovarian antigens were located in isolated feline ovarian cells by the immunofluorescence technique. Fertility-regulating effects of the developed FOA were studied. One female cat given FOA during late gestation [gestation day (GD) 49 to 51] aborted 1 dead premature fetus on day 52 and delivered 3 live offspring on GD 64. Another queen was given FOA during midgestation (GD 36 to 40) and apparently resorbed 1 of 2 conceptuses. The FOA produced in the rabbit was not organ and species specific and may cause abortion or influence fetal development in the pregnant cats.

Animals↗
PubMed1976

Immune response in dog. 3. Antibody formation in dogs and rabbits to human serum proteins and keyhole limpet haemocyanin.

Antibody formation in dogs and rabbits to human serum proteins and keyhole limpet haemocyanin (KLH) following primary, secondary and multiple stimulation was analysed. Primary injection of human serum stimulates the formation of precipitin antibodies to beta2 lipoprotein in dogs, beta2 lipoprotein and beta globulin in rabbits. After a secondary dose the rabbits formed precipitins to a whole range of human serum proteins, while the dogs to beta2 lipoprotein, albumin, beta globulin. When the primary dose of antigen was divided over a period of 8 weeks, the dog produced precipitins to beta2 lipoprotein while the rabbit to a wide range of serum proteins. Secondary stimulation of these animals did not increase the number of precipitins formed. Quantitative analysis of the antibody produced show that the best response was with beta2 lipoprotein followed by albumin and beta globulin. As the immunogenicity of the antigen was greater the differences between the two species were narrow. These differences were less pronounced following the primary injection than after the secondary and multiple stimulations. The primary response to KLH (which represents mainly IgM) is better in the dog than in the rabbit, while the secondary response (IgG) was better in the rabbit. The poorer IgG response in the dog compared to the rabbit, observed in all the experiments, is discussed.

Animals↗