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PubMed1989

[Evaluation of the reliability of the diagnostic methods in farmer's lung].

Following a study of the diagnosis of farmer's lung (PDF) carried out in 1763 active farm workers in Doubs, 294 (16.7%) were suspected of PDF and they were invited to a secondary consultation in hospital for a further work up which consisted of a clinical examination for crepitations (RC) on pulmonary auscultation (AP) and for evidence of an interstitial lung disorder (SI) on pulmonary radiograph (RP) and for evidence of a restrictive syndrome (SR) on pulmonary function tests (EFR). 238 patients (80%) accepted the additional assessment and were divided into two groups on the basis of the history and serology (precipitin tests), group 1: probable PDF (n = 65): symptoms suggestive of PDF in the presence of serum precipitins; group 2: possible PDF (n = 173): non specific symptoms with or without serum precipitins. RC were present in 21.9% of patients in group 1 and 6.4% of patients in group 2 (p less than 0.001). There was an SI in 9.2% of patients in group 1 and 4% of patients in group 2 (non significant). For the elevated radiology scores for SI there was a significant difference: 7.7% for SI in group 1 and 1.73% in group 2 (p less than 0.05). There was 38.1% of abnormal EFR in group 1 and 14.7% in group 2 (p less than 0.001) but the difference of the frequency of SR in the 2 groups was not statistically significant (9.5% in group 1 and 4.7% in group 2). In this study, an additional assessment (AP, RP, EFR) carried out at a difficult moment during winter does not appear to confirm great benefit.(ABSTRACT TRUNCATED AT 250 WORDS)

Auscultation↗
PubMed1979

A microsomal butyrylesterase appearing in rat livers during development, regeneration, and carcinogenesis, and after phenobarbital treatment.

A microsomal butyrylesterase (L-I) was purified from the livers of male W rats treated with phenobarbital, and an antiserum against this purified L-I was raised in a rabbit. By the Ouchteriony double-diffusion test, a precipitin line was observed between the anti-L-I antiserum and each Triton X-100 extract of livers during development, regeneration after partial hepatectomy, and carcinogenesis and of hyperplastic nodules and hepatomas, all of which revealed L-I in their esterase isoenzyme patterns. These precipitin lines exhibited esterase activity. The fusion of the lines of these tissue extracts and that of the purified L-I indicated the presence of an antigen site common to their esterases. The extracts of adult and fetal livers and also of hepatomas resembling fetal liver in the esterase isoenzyme pattern did not produce a precipitin line with anti-L-I antiserum.

Animals↗
PubMedDate not supplied

Tissue specificity and species cross-reactivity of porcine zona antigens isolated by gel filtration.

Antisera raised against two different doses of a major component of porcine zona pellucida isolated by gel filtration formed two precipitin lines with the components in agar double-diffusion gel. The antisera produced a positive immunofluorescence on the zona pellucida in sections of ovaries of pig, human, baboon, cow, sheep, rabbit, rat, mouse, hamster, and guinea pig. The antisera did not react with 58 different porcine tissues or five body fluids by immunofluorescence or immunodiffusion. No changes were observed in the fluorescence on the zona or in the precipitin lines when the antisera were previously absorbed with liver, erythrocytes, or plasma; however, after absorption with the porcine zona component both fluorescence and precipitin lines were completely abolished. Furthermore, control antisera against porcine erythrocyte ghosts and follicular fluid did not develop any immunofluorescence on the porcine zona. Both antisera to PZ-alpha and PZ-beta obtained by use of preparative SDS-PAGE developed the same immunofluorescence on the porcine zona shown by the antiserum to the zona component. These findings indicate that the major component of the porcine zona contains at least two zona-specific antigens, which have cross-reactivity with zona antigens of several other mammals, including humans.

Animals↗
PubMed1985

Detection of lecithin: cholesterol acyltransferase (LCAT) in a human hepatoma cell line.

A human hepatoma cell line (HepG-2) was probed for the presence of lecithin: cholesterol acyltransferase (LCAT) using an antiserum to human plasma LCAT. Double immunodiffusion analysis using antiserum to human plasma LCAT revealed a single precipitin line in the sonicated cell homogenate. This precipitin line showed a reaction of identity with highly purified plasma LCAT. The presence of LCAT within the hepatoma cells was also confirmed by an immunofluorescence test. In contrast, the cell culture supernate showed a weak and inconsistent precipitin line. These data suggest that HepG-2 cells synthesize LCAT but secretion of the enzyme by these cells into the culture medium may be partially or totally impaired.

Carcinoma, Hepatocellular↗
PubMed1988

Detection of two associated precipitating autoantibodies (DA1 and DA2) in sera from patients with systemic lupus erythematosus.

In a clinical and serological study performed on a large series of patients with different connective tissue disorders, only sera from patients with systemic lupus erythematosus (SLE) contained two precipitin systems (DA1 and DA2) directed against nuclear proteins present in a total extract of human spleen. DA1 antibody appeared in 5% of SLE patients and was always associated with DA2 antibody which was found in about 22% of SLE patients. Sera monospecific for DA1 and DA2 antibodies gave a speckled staining pattern on both rat kidney and HEp2 cells. DA1-positive patients showed a higher incidence of photosensitivity (p less than 0.001), hepatosplenomegaly (p less than 0.001), hemolytic anemia (p less than 0.05), CNS involvement, vasculitis, and diffuse proliferative glomerulonephritis than DA1-negative ones. DA2-positive patients showed an increased incidence of leukopenia (p less than 0.05) and thrombocytopenia (p less than 0.01) than controls. While several indirect evidences suggest that DA1 precipitin might be identical to the previously described MA antibody, DA2 precipitin appears as a new system in SLE. The serological association between DA1 and DA2 antibodies might be analogous to the well known ones between antibodies to Sm and nRNP and to SSA/Ro and SSB/La.

Antibodies, Antinuclear↗
PubMed1977

Indirect immunofluorescent detection of antibodies against thermophilic actinomycetes in patients with hypersensitivity pneumonitis.

With slide culture preparations of Micropolyspora faeni, Thermoactinomyces candidus, and Thermoactinomyces vulgaris used as antigens, 59 sera from patients with hypersensitivity pneumonitis and 23 sera from normal controls were studied for the presence of specific antibodies by indirect immunofluorescence and immunodiffusion methods. Of the 82 sera, 31 showed precipitins to M. faeni, five to T. candidus, and four to T. vulgaris. A group of 19 sera positive to Aspergillus antigens showed questionable reactions to thermophilic actinomycetes. The 23 sera from normal individuals were negative for specific antibodies when tested by immunodiffusion. In indirect immunofluorescence studies, we found that IgG antibodies in high titers are present only in the precipitin-positive sera whereas other antibody classes either are negative or failed to show consistent differences in titers of the positive, questionable, and control groups. The titer of IgG antibodies varied from 0 to 1:20 in the normal control group, 0 to 1:40 to 1:640 in the precipitin-positive group.

Alveolitis, Extrinsic Allergic↗
PubMed1977

Effects of ionic and nonionic detergents on antigen-antibody reactions.

Using highly sensitive and quantitative radioimmunoassay procedures we have measured the effects of different concentrations of three commonly used detergents, SDS, DOC, and Triton X-100, on antibody-antigen reactions. Triton X-100, had a relatively mild effect on primary antigen-antibody bindings, the precipitin reaction, and a double antibody RIA as evidenced by only an 8 to 10% inhibition of binding or precipitation. These results were not detergent concentration dependent, as Triton concentrations ranging from 5 to 0.1% had virtually no differential effects. Sodium deoxycholate (DOC) had a more profound effect on both primary antigen-antibody binding and the precipitin reaction than did Triton X-100, and its effects, unlike those of Triton X-100, were concentration dependent. There was a direct relationship between concentration of DOC and degree of inhibition of both primary binding and immune precepitation especially in antigen excess. Sodium dodecylsulfate (SDS), at concentrations 10- to 100-fold less than either Triton X-100 or DOC, had profound inhibitory effects on primary antigen-antibody binding, the precipitin reaction, and a double antibody radioimmunoassay. Generally, at concentrations greater that 0.01% SDS, almost all immunochemical reactivity is destroyed.

Animals↗
PubMed1975

Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia.

To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from patients with CML with that of normal subjects and patients with polycythemia vera (PRV). Antisera prepared in rabbits against granule alkaline phosphatase purified from the neutrophils of a patient with PRV produced a single precipitin line of antigenic identity when reacted with extracts of normal, PRV, and CML neutrophil granules. A histochemical stain for alkaline phosphatase activity (alpha-naphthyl acid phosphate coupled with Fast Blue RR) specifically stained the precipitin line. A variety of quantitative precipitin techniques failed to produce satisfactory precipitation of alkaline phosphatase activity. Comparative analyses were therefore performed by affinity chromatography using goat antirabbit-gammaglobulin linked to Sepharose 4B to adsorb alkaline phosphatase complexed with rabbit gamma globulin. With this method, 100% of CML, normal, and PRV alkaline phosphatase could be adsorbed. Using limiting concentrations of antibody, a proportionally smaller fraction of enzyme activity was absorbed as the concentration of PRV alkaline phosphatase or normal alkaline phosphatase was increased. Extracts of CML granules containing comparable amounts of protein but 200-fold less alkaline phosphatase activity per milligram did not specifically reduce adsorption. Thus, in CML, we found no evidence that the granulocytes contained a large amount of antigenically normal but enzymatically defective alkaline phosphatase. Examination of electron micrographs revealed no significant differences in the number or distribution of granules in the granulocytes of normal subjects or patients with PRV or CML. This suggests that the low level of neutrophil alkaline phosphatase in CML granulocytes is the result of decreased enzyme content and not a consequence of synthesis of catalytically defective enzyme.

Alkaline Phosphatase↗
PubMed1984

Serum of normal subjects contains IgG with antibody-like specificity for phospholipids.

Using counterimmunoelectrophoresis, sera from normal subjects display precipitin activity against liposomes made by phosphatidic acid, phosphatidyl ethanolamine, phosphatidyl serine and cardiolipin. No activity is detected by using liposomes made with phosphatidyl choline, sphingomyelin and phosphatidyl inositol. The same pattern of precipitation is obtained when pure IgG from normal subjects is tested against phospholipids. No precipitin activity is found by using pure IgM. The precipitin reaction is prevented by preincubating liposomes with Fab obtained from normal IgG.

Adolescent↗
PubMed1981

Immunochemical studies on heterogeneity of IgD myeloma proteins.

An antigenic heterogeneity among IgD myeloma proteins was tested by immunoelectrophoresis and double immunodiffusion in agar with four kinds of anti-delta(Fc) antisera produced by immunization with isolated Fc fragments of IgD myeloma proteins. According to antigenicity of the Fc fragment, IgD myeloma proteins were divided into two different groups. Anti-delta(Fc)-T1 (S.T.) antiserum, absorbed with te Y.S. myeloma protein or serum, either gave a faint precipitin line or failed to react against the isolated IgD myeloma proteins or sera. With the papain-digested IgD myeloma proteins and sera, anti-delta(Fc)-T1 antiserum either gave heavy precipitin lines or failed to react. Of twelve papain-digested sera containing IgD myeloma proteins tested, nine (75%) showed positive precipitin lines using anti-delta(Fc)-T1 antiserum. No relationship was found between the two groups of myeloma proteins with respect to IgD levels. SDS polyacrylamide gel electrophoresis of the IgD myeloma proteins (S.T. and Y.S.) showed no difference in the molecular weights of the whole myeloma proteins, and their light and heavy chains. Polyacrylamide gel electrophoresis of the IgD myeloma proteins (S.T. and Y.S.), after treatment with papain, revealed almost the same patterns.

Chromatography, Gel↗
PubMed1983

Isolation and identification of the third component of complement of Japanese quails.

The identification of the third component of complement (C3) of Japanese quails was attempted by using rabbit antiserum prepared against quail serum-treated zymosan (ZX) as an initial reagent. This antiserum (anti-ZX) had agglutinating activity on rabbit erythrocytes reacted with quail antibody and quail complement (EACq) but not on EAq, and developed two precipitin lines against quail serum at beta- and gamma-regions in crossed immunoelectrophoresis. Subsequently, monospecific antisera to each of these precipitin lines were prepared in rabbits, and quail serum proteins reactive with these antisera were purified by salt precipitation followed by Sephadex gel filtration and DEAE cellulose column chromatography. One protein with a m.w. of 184,000 (184K) resembled mammalian C3 in that: 1) monospecific antiserum (anti-184K protein serum) agglutinated EACq but not EAq; 2) treatment of fresh quail serum with either inulin or zymosan resulted in the conversion of the precipitin line developed against 184K protein from gamma to beta in crossed immunoelectrophoresis; 3) the 184K protein was shown to consist of two polypeptide chains of 110K and 73K linked by disulfide bonds. Furthermore, the 184K protein in serum was cleaved through the incubation with inulin to 174K and 140K proteins that might correspond to C3b and C3c of human complement; 4) the 184K protein bound to zymosan was eluted with hydrazine or methylamine but not with Nonidet P-40, indicating that 184K protein binds to zymosan by a covalent bond but not by a hydrophobic one; and 5) by treatment of fresh quail serum with methylamine, complement reactivity was reduced, although its activity was restored by the addition of purified 184K protein. These results suggest the 184K protein is the quail's equivalent to mammalian C3. When quail serum was reacted with cells that had complement-activating capacity, quail C3 deposited on their membrane as in mammalians; however, no conversion of quail C3 was noted by the reaction with CVF. Antibody to quail C3 failed to cross-react with that in mammals.

Animals↗
PubMed1984

Cartilage link proteins. Biochemical and immunochemical studies of isolation and heterogeneity.

Native and clostripain-derived link proteins from proteoglycan aggregates were separated by gel chromatography in 4 M guanidine HCl from low-buoyant-density proteoglycan and proteoglycan hyaluronic acid-binding region after extraction from adult bovine nasal cartilage and the Swarm rat chondrosarcoma. Separations were monitored with Laurell immunoelectrophoresis using precipitating antibodies to link protein, hyaluronic acid-binding region, and low-buoyant-density proteoglycan. These immunoanalyses, with sodium dodecyl sulfate-polyacrylamide gel analyses, revealed the usefulness of this combined approach when assessing the purities and identities of these molecules. Using these isolated link proteins we provide data suggesting the presence of two immunologically detectable forms of link proteins of the same molecular weight. On immunoelectrophoresis both rat and bovine link proteins of a single molecular weight each produced two precipitin reactions with antibody to link protein. They were of similar intensity for native molecules but of different intensity for clostripain-isolated link protein. Isoelectric focusing in 6 M urea revealed that the 48,000 and 44,000 molecular weight link proteins of bovine nasal cartilage together produce a complex pattern of many bands. Link proteins of a single molecular size produced a much simpler, predominantly five-banded focusing pattern. Immunoelectrophoresis of the electrofocused clostripain rat link protein (42,000) revealed that the three major central bands each produced double precipitin reactions. Mixing of native and clostripain-derived link protein in 4 M guanidine HCl followed by dialysis to 6 M urea prior to isoelectric focusing did not change the focusing position of the individual bands. This suggests that the heterogeneity of focusing forms was due to the existence of different isoforms. The double precipitin reactions may be due to the existence of two different conformations expressing different epitopes of the kind reported previously by Thonar et al. (Thonar, E. J.-M. A., Kimura, J. H., Hascall, V. C., and Poole, A. R. (1982) J. Biol. Chem. 257, 14173-14180).

Animals↗
PubMed1984

Immunochemical studies on human monoclonal macroglobulins with specificities for 3,4-pyruvylated D-galactose and 4,6-pyruvylated D-glucose.

Four of six human monoclonal IgM proteins were found to react best with Klebsiella polysaccharides containing 3,4py beta DGal (pyruvic acetalated D-galactopyranose), one with Klebsiella polysaccharides with 4,6pyDGlc; the sixth is uncharacterized. The combining sites of two of these (IgMWEA and IgMNAE) were essentially indistinguishable by quantitative precipitin studies at varying pH and by quantitative precipitin inhibition assays, but the other two differed in specificity of their combining sites from these and from each other. These differences were detected by precipitin inhibition assays with 3,4py beta DGal-containing oligosaccharide alditols, the R and S isomers of methyl 4,6py alpha DGal, the R isomer of methyl 4,6py beta DGal, or the R and S isomers of methyl 4,6py alpha DGlc, and -beta DGlc. In all of these except the S isomer of methyl 4,6pyDGal and R isomer of methyl 4,6pyDGlc, the carboxyl group is axial to the plane of the acetal ring. Their specificity appears to be determined by the nonreducing ends of chains and is considered to be cavity-type.

Antibody Specificity↗
PubMed1977

Relationship of contact activation cofactor (CAC) procoagulant activity to kininogen.

Contact activation cofactor (CAC) facilitates the interaction of factors XI and XII. Patients lacking CAC have a coagulation defect and are deficient in high molecular weight kininogen. The coincidence of these two defects suggests that a single protein may be responsible for both physiologic functions. Immunologic and activity studies have been made on isolated CAC to clarify the relationship between CAC and kininogen. CAC forms a single precipitin line with anti-human kininogen, and antikininogen neutralizes CAC activity. CAC and high molecular weight kininogen show a reaction of identity on immunodiffusion against rabbit anti-CAC. Anti-CAC forms two precipitin lines with normal plasma which can be identified as high and low molecular weight kininogen. Monospecific immunoabsorbed anti-CAC forms a single precipitin line with plasma high molecular weight kininogen and neutralizes CAC activity. Cleavage of kinin fragment from CAC by insoluble trypsin or kalikrein does not proportionally reduce procoagulant activity. CAC neutralized by anti-CAC can release kinins on exposure to trypsin or kallikrein. The results support the conclusions that CAC procoagulant activity is a function of high molecular weight kininogen, that antigenic determinants unique to high molecular weight kininogen are shared by the CAC portion of the molecule, and that the clotting reactions may occur at a site removed from the kinin peptide.

Animals↗
PubMedDate not supplied

[Immunochemical properties of secretory IgA of human colostrum].

Immunochemical properties of secretory IgA obtained from the colostrum of healthy post-partum women are discussed. Lipids were completely eliminated by centrifugation and the supernatant was adjusted at pH 8.0 with NaOH and dialysed against a PBS buffer. Fractionation through a Sephadex G-200 column was fractionated again through a DEAE-cellulose column which eluted only pure IgA. Aliquots of 3 ml each were checked for protein content in an Uvicord spectrophotometer at 254 millimicron. Three fractions were obtained from the Sephadex column, the first involving tubes 50 to 90 contained IgA and IgM, the second from tubes 91 to 120 contained IgG and the third from tubes 130 to 150 contained alfa-lactalbumin and lactotransferrin. Passage of fraction I through a DEAE-cellulose column led to the collection of pure IgA in tubes 45 to 80 with the highest content in tube 53 which was employed in the immunization of rabbits. Ouchterlony immunodiffusion and immunoelectrophoresis were employed to check the reactivity among whole colostrum as well as Sephadex and DEAE-cellulose fractions against an anti-IgA, anti-IgM, anti-IgG, anti-immunoglobulins and anti-whole human sera. Several precipitin bands revealed that human colostrum contained IgA, IgG, and IgM. Pure secretory IgA was used to immunize adult rabbits with complete and incomplete Freund's adjuvant for a period of two months. A rabbit anti-IgA serum was then obtained and after being purified by saline precipitation and dialysis and passed through a DEAE-cellulose column, was labeled with I-131 reaching a specific activity of 20 microCi/mg. This antiserum was used against human colostrum, normal serum and saliva, and serum and urine from a patient with an IgA myeloma confirmed by means of precipitin methods and autoradiographies. Chemical purity of the secretory IgA was confirmed by analytic ultracentrifugation obtaining a sedimentation value of S 20: 10.5. In all cases a single precipitin band was obtained in spite of the low concentration of the antigens; the isotopic labelling did not alter the specificity and the sensitivity of the antiserum and its usefulness was well established. The biological properties of secretory IgA are described and its importance in local immunity is emphasized.

Antibodies, Anti-Idiotypic↗
PubMed1980

[Further observations on the use of counterimmunoelectrophoresis (CIEP) on cellulose acetate membrane (Cellogel) in the diagnosis of visceral leishmaniasis (author's transl)].

Technique of counterimmunoelectrophoresis (CIEP) on cellulose acetate membrane (Cellogel) is described for diagnosis of (human and canine) visceral leishmaniasis (VL). Various lots of antigen were grossly obtained from the liquid phase (10, 20 and 30 tubes respectively) of cultures of Leishmania donovani by repeated freezing and thawing. Sera from patients (and, in a few cases, dogs) with confirmed VL, other parasitic and non-parastic diseases (especially blood disorders and hepatosplenomegaly) and from blood donors were tested. Positive results were obtained in 91-93% (according to various lots) of the patients with VL. All sera from infected dogs gave positive results. No precipitin lines were detected in the control sera. Antigens from 30 (or 20 tubes) showed better results with regard to the evidence of the precipitin lines. Clarity of the precipitin bands appears to be in relation to: 1. the protein concentration of the antigens; 2. the antibody levels of the sera. CIEP on cellulose acetate membrane combine the features of good sensitivity, specificity and speed of performance and appear available for use also in epidemiological research.

Animals↗
PubMed1981

Isolation of Moraxella bovis ribosomes and their subsequent use in a vaccine against infectious bovine keratoconjunctivitis.

A study was conducted to determine whether a Moraxella bovis ribosomal vaccine would protect calves from infectious bovine keratoconjunctivitis (IBK). Each of 16 calves were given 2 inoculations 21 days apart. Twenty-one days after the 2nd inoculation, 8 of the calves were challenge exposed with a homologous strain culture and 8 calves were challenge exposed to a heterologous strain culture of M bovis. Sedimentation velocity analysis of the ribosomes used in this study indicated that they were mostly 30S and 50S subunits. Chemical assays indicated that the ribosomes were composed of 64% to 65% RNA and 35% to 36% protein. The cesium chloride buoyant density of the ribosomes was 1.62 g/ml. Ribosomes used as antigen gave 1 line of precipitation in a gel-diffusion precipitin test with hyperimmune serum against the whole-cell antigen of the homologous strain of M bovis. The eyes of all the experimentally exposed calves became infected and all calves developed clinical signs of either unilateral or bilateral IBK. None of the sera of the vaccinated calves had detectable precipitins against the ribosomal antigen at the time they were challenge exposed, but most of the sera had precipitins against whole-cell and pilus antigens. The results indicate that M bovis ribosomes, although similar to other bacterial ribosomes, did not protect cattle against IBK.

Animals↗
PubMed1980

Studies on human heart citrate synthase.

Citrate synthase from human heart was purified by affinity chromatography with Sepharose-ATP. The molecular weight (100,000) and the presence of two presumably identical subunits do not differ from other mammalian citrate synthases. However, the kinetics constants and immunologic characteristics of the enzyme differed from other mammalian citrate synthases. The Km values for acetyl-CoA (0.4 microM) and oxaloacetate (0.25 microM) were about an order of magnitude lower than those previously found for other mammalian (and eucaryotic) citrate synthases. The kinetics constants for the reverse reaction Km for citrate (420 microM) and CoA (70 microM), were of similar magnitude to the values for other mammals. Anti-human heart antiserum developed a single precipitin line in an Ouchterlony plate against a heart extract, no precipitin line with brain, and a precipitin line with spurs against liver and kidney extract. Following myocardial infarction in men, the enzyme appeared in peripheral blood rarely and in low concentration in contrast with earlier experiences with experimental infarction in dogs.

Animals↗