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Biomedical subjects

J A Price

Publications and source records attributed to J A Price.

At least 55 records · Page 3Linked to original sources
PubMed1988

ELISA method for measurement of airborne levels of major laboratory animal allergens.

Three types of air-sampling apparatus (the Air-Sentinel, Burkard Personal Sampler and Casella Personal Sampler) were compared for their use in sampling the air in situations where individuals are exposed to laboratory animals, and a cascade impactor was used to determine the sizes of particles carrying the allergens under investigation. An ELISA, using monospecific antisera raised to selected major allergens of the mouse, rat and rabbit, i.e. mouse Ag 1 (mouse urinary prealbumin), rat Ag 4 (rat urinary prealbumin) and rabbit Ag R1, was developed to assay the extracts obtained from the samplers. This ELISA system was able to detect greater than 5 ng/m3 of allergen in sampled air. The rat and mouse allergens were shown to be carried mainly on particles of 6-18 micron, whereas the rabbit allergen was also found on particles of 2 micron and smaller. Allergen levels correlated well with the number of animals present in the room and the degree of activity during sampling. A protective filtered-air hood, when worn during surgical operation procedures, was shown to reduce effectively the level of rat allergen breathed by an individual.

Air Pollutants↗
PubMed1988

Allergy to rabbits. II. Identification and characterization of a major rabbit allergen.

Quantitative immunoelectrophoretic techniques have been used to study the antigenic components found in extracts of dust collected from rabbit housing areas. To determine the possible source of these antigens, comparisons have been made to rabbit saliva, urine, fur and dander. Specific antisera for the rabbit extracts were raised in guinea pigs. One major component of the dust (Ag Rl) was also found in large amounts in saliva, slightly less in fur and in only minimal amounts in urine and dander. Crossed radioimmunoelectrophoresis (XRIE) of the dust, performed with sera from 14 rabbit allergic individuals who were RAST positive to rabbit saliva, urine and dust identified four IgE-binding constituents. Individual responses varied but all sera reacted with Ag Rl, identifying this as a major rabbit allergen. Dust RAST inhibition studies with rabbit dust, saliva and urine indicated saliva to be closely related to the dust. Ag Rl is a glycoprotein which appears to be very heterogeneous in nature. It produced a broad biphasic precipitin peak on immunoelectrophoresis and eluted from Sephacryl S-200 gel filtration over the molecular weight range 30-50 Kd, although a molecular weight of 17 Kd was indicated by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gradient gel electrophoresis. The RAST inhibition results and the antigenic similarity of saliva to the dust suggest this to be the most likely source of the major rabbit allergen, Ag Rl.

Allergens↗
PubMed1987

Changes in cell surface charge and transmembrane potential accompanying neoplastic transformation of rat kidney cells.

Free flow electrophoresis measurements have been used to determine the surface charge density of normal rat kidney (NRK) cells and a clone of NRK, designated as 6m2, that exhibit a transformed phenotype at 33 degrees C and a non-transformed phenotype at 39 degrees C. A clone of 6m2, designated 54-5A4, which is transformed at both 33 degrees C and 39 degrees C was also studied. A surface charge density of -1.42 microC/cm2 was obtained for the NRK and non-transformed 6m2 cells at 39 degrees C, whereas at 33 degrees C values of -1.85 and -1.78 microC/cm2 were determined for the transformed 6m2 and 54-5A4 cells, respectively. It was found that 72% of the increased charge that appeared on the transformed 6m2 cells compared with the non-transformed 6m2 cells was RNAase sensitive. The time-dependent decrease in surface charge that accompanied the shift of the 6m2 cells from their transformed to non-transformed state was found to mirror the increase in transmembrane potential previously reported using a fluorescent dye technique, and was also comparable to the reported temporal changes in their morphology and virally-coded protein content.

Animals↗
PubMed1987

Allergy to mice. I. Identification of two major mouse allergens (Ag 1 and Ag 3) and investigation of their possible origin.

An extract of dust from the outlet filters of a mouse isolator was used as a basis for determining the source of inhalant allergens for subjects sensitive to this species. The antigenic components, identified by crossed immunoelectrophoresis (XIE), were compared to those found in extracts of other mouse-derived source materials, i.e. urine, fur, dander and saliva. Of the eight dust components, one (Ag 1) was identified as antigenically identical to the major urinary pre-albumin whilst the others were detected in fur, and to a lesser extent dander and saliva. None of the dust antigens was detected as a component of food or bedding. Crossed radio-immunoelectrophoresis (XRIE), performed using sera from a group of fifteen mouse-allergic subjects (positive by RAST to mouse extracts), identified seven of the dust antigens as IgE-binding components. Antigens 1 and 3 were reactive with all the sera tested and have, therefore, been termed the 'major' allergens. Varied responses were obtained to the other 'minor' antigens. Ag 1 (urinary pre-albumin) and Ag 3 were detected in all samples of mouse dust studied. RAST and RAST inhibition also indicated the presence of urinary pre-albumin. These findings suggest that the major mouse inhalant allergens may be derived predominantly from urine and secretions originating in the skin and present on the fur.

Allergens↗
PubMed1987

Allergy to laboratory animals: characterization and source of two major mouse allergens, Ag 1 and Ag 3.

Using quantitative immunoelectrophoretic methods, two major allergenic components, Ag 1 and Ag 3, have been identified in extracts of mouse dust. Both antigens were of similar electrophoretic mobility and molecular weight (20-25 kilodaltons). However, Ag 1 proved to be antigenically identical to mouse urinary prealbumin, whilst Ag 3 was shown immunohistochemically to be present within the hair follicle and on the stratum corneum.

Allergens↗
PubMed1986

Surface charge measurements on Micrococcus lysodeikticus and the catalytic implications for lysozyme.

Electrophoresis measurements on Micrococcus lysodeikticus have shown that the net surface charge density on the cell wall is constant at around -1.5 microC/cm2 for the pH range 4-8. This result has enabled a quantitative analysis to be made of how the electrostatic field associated with the negatively charged cell wall influences the ionic strength and pH dependency of the lytic activity of lysozyme towards M. lysodeikticus. A dominant effect is the creation of a local pH gradient at the cell wall, and at high ionic strengths the lytic activity is found to be controlled by an electrostatic force of attraction between the lysozyme molecule and the cell wall. As the ionic strength of the supporting electrolyte is decreased, however, an electrostatic force of repulsion becomes dominant and is associated with a negative charge carried by the lysozyme molecule, which could possibly be the ionized Asp-52 residue at the active site. This is considered to arise from the fact that at low ionic strengths the fine details of the heterogeneous charge distribution on the cell wall and lysozyme molecule are only partially screened by counter ions.

Chemical Phenomena↗
PubMed1986

Allergy to rabbits. I. Specificity and non-specificity of RAST and crossed-radioimmunoelectrophoresis due to the presence of light chains in rabbit allergenic extracts.

Investigations have been carried out into the presence of antibody light chains in rabbit allergenic extracts and the interference in RAST and crossed-radioimmunoelectrophoresis (XRIE) caused by antibodies directed against them. A "non-specific" uptake of radioactivity in XRIE has been demonstrated to be caused by direct cross-linking of the 125I rabbit anti-human IgE by the sheep antibodies in the immunoprecipitate of rabbit light chains. Preincubation with normal rabbit serum blocked this direct uptake of the labelled antibody and enabled specific IgE uptake on the light chains to be demonstrated for rabbit allergic sera. Verification of the allergenicity of the light chains was obtained from a specific light chain RAST. Elution from a Sephacryl S-200 gel filtration column indicated a MW of approx. 50 Kd and confirmation of the component as light chain dimers, not Fab fragments, was obtained by allotyping for loci present on heavy chains and light chains in the Fab region. Light chains were detected in urine from rabbits of all ages and in an extract of dust collected in a rabbit housing area. No background staining was observed in XRIE using rabbit antisera, either with rabbit allergic sera with specific IgE or with a human serum containing specific IgG antibodies to rabbit IgG. This latter serum also showed no evidence of uptake on all immunoprecipitates in systems using rabbit antisera, and did not give false positive RAST results when the labelled rabbit anti-human IgE contained unlabelled rabbit IgG. Those sera with specific IgE to light chains showed no uptake in XRIE using rabbit antisera, indicating that the IgE was possibly specific for epitopes revealed by the dissociation of the whole IgG molecule.

Allergens↗
PubMed1983

The release of 3-methyladenine from nucleosomal DNA by a 3-methyladenine DNA glycosylase.

Nucleosomes from chicken erythrocytes, with DNA containing an average of 144 base pairs, were alkylated with [3H]methylnitrosourea. The level of alkylation of the nucleosomal DNA was 48% of that of free DNA. The histones had approximately one tenth the radioactivity of the DNA. There was no statistically significant difference between alkylation of nucleosome bases in the major vs. minor groove. When the first 50 residues of the alkylated nucleosomal DNA were examined on sequencing gels, the 7-methylguanine and 3-methyladenine (3-MeA) residues were distributed randomly. The 3-MeA DNA glycosylase I of E. coli was used to measure the release of 3-MeA from nucleosomal DNA. Incubation at 37 degrees C resulted in a release which reached a plateau of approximately 33% of the 3-MeA groups of the nucleosomal DNA. A partially purified 3-MeA DNA glycosylase from rat liver gave similar results. The limited enzymatic release is most likely due to steric hindrance of the enzyme by the DNA-histone interactions on the surface of the core particle. An alteration of nucleosomal conformation has been suggested as an explanation for repair of nucleosomal DNA. Two model systems have been examined. The addition of ethidium bromide to alkylated nucleosomes increased the enzymatic release of 3-MeA to approximately 75% and altered the electron microscopic appearance. The chemical alkylation of nucleosomes also increased the enzymatic release of 3-MeA as well as decreased the sedimentation coefficient. All of these experiments indicate a limited availability of 3-MeA residues to the glycosylase and suggest that some conformational change must occur in vivo for complete repair.

Adenine↗
PubMed1982

Inhibition of concanavalin A response during osteopetrosis virus infection.

Infection of animals with oncogenic viruses frequently leads to an immunosuppressed state. We have examined immunosuppression induced by an avian osteopetrosis virus, myeloblastosis-associated virus of subgroup B inducing osteopetrosis [MAV-2(O)], and our results suggest that this virus induces immunosuppression by a novel mechanism. Lymphoid cells from osteopetrotic chickens did not respond to a wide dose range of concanavalin A (Con A) over a wide cell density range. Failure to undergo blastogenesis was not due to a lack of Con A-binding sites, since 125I-labeled Con A bound to lymphocytes from infected and uninfected chickens. Infected lymphocytes failed to respond to sodium metaperiodate stimulation, indicating that failure of blastogenesis was not due to a blockage of Con A receptor sites. MAV-2(O) infection of chicks 8 days of age resulted in a transient immunosuppression which appeared 1 to 2 weeks after infection. Cell-mixing experiments showed that MAV-2(O)-induced immunosuppression was not attributable to suppressor cells. In contrast, adherent cells from normal lymphoid preparations restored mitogenicity to lymphocytes from MAV-2(O)-infected animals. Adherent cells were present in the spleen and peripheral blood lymphocytes of MAV-2(O)-infected chickens in numbers comparable to those of the uninfected animal, and both sets of cells contained Fc-dependent phagocytic activity and nonspecific esterase. Peritoneal exudate cells were elicited from osteopetrotic and normal chickens in similar numbers. We conclude that MAV-2(O) induces immunosuppression by interfering with an accessory function of macrophage-like adherent cells.

Anemia↗
PubMed1981

Influence of bursectomy on bone growth and anemia induced by avian osteopetrosis viruses.

This study examines the contribution of the bursa of Fabricius to the pathogenic manifestations of two myeloblastosis-associated viruses which primarily cause osteopetrosis [MAV-1(O) and MAV-2(O)]. MAV-2(O) infection of surgically bursectomized 1-month-old chicks resulted in a rapidly fatal anemia whereas infection of untreated chicks of the same age resulted in a transient drop in hematocrit. Surgical bursectomy of embryos before or after embryonal infection with MAV-2(O) did not alter the course of osteopetrosis, indicating that the bursa was not a source of target cells. Bursectomy prolonged the period of susceptibility to MAV-2(O) induced osteopetrosis until one day posthatching; untreated chicks were not susceptible to osteopetrosis induction at that age. MAV-1(O) infection of eight-day-old bursectomized chicks resulted in osteopetrosis in the absence of anemia; untreated eight-day-old chicks infected with MAV-1(O) showed no effects of virus infection. A role for the bursa in MAV-2(O) infection was found in the participation of neutralizing antibodies in the recovery from anemia. A single dose of antiviral antibody was found to prevent the appearance of anemia. The protective effect of antiviral antibody was dose dependent, and antiserum administration had to be initiated within three days after virus in order to be effective. Antiviral antibody against MAV-1(O) did not protect against MAV-2(O)-induced anemia, suggesting subgroup specificity. These results suggest that the bursa does not provide a stem cell which participates in the bone hyperplasia induced by MAV-1(O) and MAV-2(O). Rather, the humoral antibodies provided by cells derived from the bursa may serve to eliminate viremia and limit virus-specific cytopathogenic effects.

Age Factors↗
PubMed1980

Fractionation and reconstitution of vitamin K-dependent carboxylation activity in rat liver microsomes.

Attempts to purify the vitamin K-dependent carboxylation system from rat liver microsomes have not yet met with success. Purification procedures result in low yields of activity even after relatively mild separation methods. We have been able to demonstrate that one reason for these failures is that there are at least two components (which can be separated) necessary for the reaction. Recombination of the separated components is possible if the detergent (Triton X-100) concentration is lowered and ethylene glycol is added to the system. Under these conditions, vitamin K-dependent carboxylation of synthetic pentapeptide (Phe-Leu-Glu-Glu-Leu) can be totally reconstituted.

Animals↗
PubMed1978

Laetrile--an overview.

The original theory in the 1920s on the mode of action of Laetrile is described along with the research that followed in light of this theory. For over 40 years, studies were conducted, using test animals, in an attempt to substantiate the theory. All of these studies have shown Laetrile does not preferentially kill cancer cells. In spite of these studies, the misconception persists that Laetrile prevents and cures cancer. The legal and socioeconomic implications of Laetrile are examined and the role of health education in combating this problem is explored.

Amygdalin↗