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Biomedical subjects

N J Calvanico

Publications and source records attributed to N J Calvanico.

9 recordsLinked to original sources
PubMed1979

An animal model of hypersensitivity pneumonitis in rabbits. Development of chronic pulmonary inflammation and cell-mediated hypersensitivity after repeated aerosol challenge.

Chronic pulmonary inflammation was produced in immunized rabbits by repeated aerosol exposure to soluble antigen. The pulmonary inflammatory response was correlated with the development of cell-mediated hypersensitivity in the lung as evaluated by migration-inhibition studies using bronchoalveolar cells. Such inflammation could be produced with either pigeon dropping extract, an etiologic agent of hypersensitivity pneumonitis, or with human gamma globulin. Development of the inflammatory response was immunospecific and could not be transferred to normal recipients with large quantities of immune serum. Collectively, these data suggest that the development of pulmonary inflammation was due to a cell-mediated immunologic reaction in the lung.

Aerosols↗
PubMed1979

IgA and IgG antibody activities of serum and bronchoalveolar fluid from symptomatic and asymptomatic pigeon breeders.

Serum IgA and IgG antibody activities against pigeon serum were measured in 16 symptomatic pigeon breeders, 20 asymptomatic pigeon breeders, and 3 normal subjects by radioimmunoassay. The IgA and IgG antibody activities against pigeon antigen of the group of patients with disease was significantly greater than those of patients in the asymptomatic and the control group. The overlap of results for the symptomatic and asymptomatic breeders limits the diagnostic value of these individual IgA or IgG antibody determinations. Bronchoalveolar fluid and serum samples from a smaller group of pigeon breeders who underwent lung lavage were available for studies of antibody activity against pigeon serum. Ten asymptomatic and 6 symptomatic breeders were available for study. Both IgG and IgA antibody activities were detected by radioimmunoassay in serum samples and bronchoalveolar fluid. The IgA antibody activity determined by the radioimmunoassay was higher in the respiratory secretions.

Alveolitis, Extrinsic Allergic↗
PubMed1979

Bullous pemphigoid antigen. II. Isolation from the urine of a patient.

This report concerns the isolation of bullous pemphigoid antigen from the nondialyzable urinary components of a patient with the disease. The isolation was accomplished by ion exchange chromatography and gel filtration. Pemphigoid antigen was found to be a basic glycoprotein that on SDS gel electrophoresis showed two major bands, one in the 18,000 m. w. region and the second with a m. w. of 74,000. Between these two bands, two additional bands appeared; one of 35,000 daltons and the other of 68,000 daltons. The 18,000 m. w. band was eluted from the gel and rerun on SDS gels. These gels showed the 18,000 m.w. band and also the appearance of the 35,000 and 74,000 m.w. bands. This finding indicates that urinary pemphigoid antigen may exist both as a single monomeric form and in polymeric aggregates.

Animals↗
PubMed1978

Studies on extracellular proteases of Streptococcus sanguis. Purification and characterization of a human IgA1 specific protease.

Extracellular caseinolytic activity was found in the culture fluid of Streptococcus sanguis ATCC 10556 grown in a dialyzed culture medium. This activity was due to multiple proteases that differed in their elution from hydroxyapatite, sensitivity to enzyme inhibitors, specificity and optimum pH. IgA protease, which splits human immunoglobulin A1 into intact Fc and Fab could be effectively separated from these relatively non-specific proteases and purified to apparent homogeneity in 20% yield by a five-step procedure. Although the bulk of the dextran sucrase activity was separated from the IgA protease, a small amount of sucrase activity remained with the final IgA protease preparation. In polyacrylamide gel electrophoresis at pH 9.5 both activities were located in the single protein band detected in this preparation. A quantitative method for the assay of IgA protease was developed, based on radial immunodiffusion to quantitate the Fab produced. This was used to follow the specific activity and yield during purification, and to characterize some of the catalytic properties of the enzyme. At an enzyme/substrate ratio of 1: 400 (w/w) the protease could effect 50% proteolysis of IgA in overnight incubation at 37 degrees C. The optimum activity was at pH 8.0, and 50% inhibition was achieved at 4 . 10(-4) M o-phenanthroline or 8 . 10(-4) M ethylene diamine tetraacetate. Concentrations of diisopropyl phosphofluoridate, phenylmethyl-sulfonyl fluoride, iodoacetate and p-chloromercuribenzoate up to 10(-2) M were without effect on the IgA protease activity. Full reactivation of the chelator inhibited enzyme could be achieved by the addition of Mg2+, Mn2+ or Ca2+.

Edetic Acid↗
PubMed1978

Phylogenetic studies with pemphigus and pemphigoid antibodies.

Indirect immunofluorescence (IF) studies were performed on skin from a variety of vertebrate specimens and IgG fractions from pemphigoid and pemphigus sera. Pemphigoid antigen was present in fish, amphibian, reptilian, avian and mammalian skin, whereas pemphigus antigen was observed in avian and mammalian skin only.

Animals↗
PubMed1977

Separation of epidermis from dermis with sodium thiocyanate.

After human skin is treated with 2 N sodium thiocyanate, epidermis is easily separated from dermis. The level of cleavage occurs at the lamina lucida of the basement membrane zone. Bullous pemphigoid antigen remains attached to the epidermis.

Histological Techniques↗
PubMed1977

Bullous pemphigoid antigen: isolation from normal human skin.

A protein moiety from epidermal PBS-soluble products was isolated by gel filtration (Bio-Gel A-1.5m) and ion exchange chromatography (DEAE-cellulose). This protein (A-1-Epid) was not retarded by DEAE-cellulose in Tris-HCl buffer, 15mM, pH 8.1. By IEP against an antiserum to epidermal antigens, it showed a single cathodal arc. On disc electrophoresis, at low pH (4.3) a single band was apparent. On SDS gels this protein demonstrated two bands, one with a molecular weight of 20,000, and the second with a molecular weight of 9,200. This purified antigen was able to block the staining of the basement membrane zone produced by bullous pemphigoid antibodies on monkey esophagus and normal human skin with the use of indirect immunofluorescence. This study also demonstrates that bullous pemphigoid antigen (A-1-Epid) and a second epidermal protein (A-2-Epid) are present in the PBS-soluble products of human esophageal mucosa, saliva, and urine. These antigens appear to be unrelated with the blood group substances or secretor status of the donors.

Animals↗
PubMed1977

PBS-soluble substances with blood group activity from human epidermis and dermis.

Phosphate-buffered saline (PBS) soluble extracts of human epidermis and dermis from secretor donors contain products with blood group antigenic activity. The predominant blood group in a sample was the same as the red cell phenotype of the donor. H substance activity was present in all PBS-soluble products (from A, B and O donors). By gel filtration chromatography on a Bio-Gel A-1.5 m column; the epidermal and dermal PBS-soluble blood group substances fractionate in the void volume.

Blood Group Antigens↗