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Biomedical subjects

N R Rose

Publications and source records attributed to N R Rose.

At least 199 records · Page 11Linked to original sources
PubMed1979

Acid phosphatase: new developments.

Acid phosphatase was the first "tumor marker" to be measured in the blood, and over 40 years have passed since an elevation of the serum acid phosphatase level was observed in patients with prostatic carcinoma. However, significant elevations in the level of this enzyme have been observed in other diseases, as well as elevations of other tissue phosphatases. Many improvements in the colorimetric technique have been introduced, but none has been used successfully to detect the tissue origin of this ubiquitous enzyme. The finding that prostatic acid phosphatase is antigenically distinct from acid phosphatase of other tissues opened a new horizon in the measurement of acid phosphatase in prostatic cancer. On the basis of this immunochemical specificity, several immunoassays have been employed for determining the prostatic acid phosphatase level.

Acid Phosphatase↗
PubMed1979

Influence of major histocompatibility haplotype on autoimmune disease varies in different inbred families of chickens.

Three partially inbred substrains of Obese strain chickens were studied for the spontaneous development of autoimmune thyroiditis. The influence of the major histocompatibility complex (B haplotype) was marked in one, less marked but still significant in a second, and barely detectable and transient in a third substrain. These differences in the effect of B haplotype may be due to the overriding action of genes other than those within the B haplotype.

Animals↗
PubMed1979

Effect of Freund's complete adjuvant on the immune response of vasectomized rats.

Rats were vasectomized, vasectomized and injected in the epididymis with Freund's complete adjuvant (FCA), or only injected with FCA without vasectomy. All were positive for sperm agglutinins, in contrast to sham-operated or untreated controls. Generally, the highest titers were found in vasectomized or unoperated animals given FCA, indicating that local granuloma formation promotes the production of sperm autoantibody, even in nonvasectomized rats.

Animals↗
PubMed1979

Kinetics of cellular and humoral response of rabbits immunized with mycoplasma pneumoniae.

The cellular and humoral responses of rabbits immunized with Mycoplasms pneumoniae antigen in saline or incorporated in Freund's complete adjuvant were examined. Peripheral blood leukocytes were used for the leukocyte migration inhibition (LMI) test. Both groups of animals showed significant LMI activity in the presence of M. pneumoniae as well as cross-reacting M. salivarium antigens but response to M. pneumoniae antigen was more pronounced. In the humoral response no such cross-reactivity was observed. Although some of the animals (3/8) demonstrated antibodies to M. salivarium prior to immunization the titers were not influenced by the immunization with M. pneumoniae antigen. Both groups of animals produced antibodies to M. pneumoniae antigen only, but significantly higher titers were observed in the adjuvant group. Cold hemagglutinins in both groups appeared earlier than the specific antibodies to mycoplasma. The adjuvant had no effect on the production of the cold agglutinins.

Agglutinins↗
PubMed1979

Regulation of autoimmune response to mouse thyroglobulin: influence of H-2D-end genes.

Studies were initiated to define the H-2-linked genetic control of response to self-determinants of MTg. In addition to the Ir gene control of H-2K end, a modifying effect of D end was seen. The extent of regulation depended upon the derivation of the K-end Ir-Tg gene(s) as well as the D-end genes. When the Ir-Tg gene was from good responder H-2k and H-Ss strains, and the H-2D-end gene from the d allele, antibody levels were moderate to high but cellular infiltration was significantly reduced. These findings demonstrate genetic interaction between I-region and D-end gene products in the response to a self-antigen, MTg.

Alleles↗
PubMed1978

Bone marrow acid phosphatase in staging of prostatic cancer: how reliable is it?

To evaluate the reliability of bone marrow acid phosphatase in the staging of prostatic carcinoma we analyzed 50 bone marrow samples collected at random from the hematology service at this hospital. The samples were assayed for acid phosphatase content by a colorimetric method using sodium thymolphthalein monophosphate as a substrate and by 2 immunochemical assays developed at our laboratory (counter immunoelectrophoresis and radioimmunoassay). We found a high percentage (61 per cent) of falsely positive results in patients with various hematological diseases without evidence of prostatic carcinoma by the colorimetric evaluation. All of these patients except 1 had negative immunochemical assay. Until a specific assay for prostatic acid phosphatase is developed for clinical use we caution the use of a single elevation of bone marrow acid phosphatase as a parameter of metastatic disease.

Acid Phosphatase↗
PubMed1978

Purification and characterization of human prostatic acid phosphatase.

Human prostatic acid phosphatase (orthophosphoric monoester phosphohydrase, EC 3.1.3.2) is purified to homogeneity by standard procedures which include CM-Sephadex, Con A affinity chromatography and gel filtration. The purified enzyme is antigenically specific and has a M.W. of 100,000 with subunit M.W. of 48,000. However, the enzyme exhibited charge heterogeneity. Two major electrophoretic or chromatographic isozymic forms of PAP were separated by DEAE-Sephadex chromatography and their immunochemical identity was studied by immunodiffusion before and after the neuraminidase digestion. Quantitative precipitin and inhibition experiments showed immunological identity of the two chromatographic isozymes. Immunologic specificity of this enzyme resides on the protein moiety rather than the carbohydrate residue, although the latter group is mostly responsible for the charge group heterogeneity of the enzyme.

Acid Phosphatase↗
PubMed1978

Human prostatic acid phosphatases: I. Isolation.

A new purification procedure is described for the human prostatic acid phosphatase. The procedure included carboxy-methyl-Sephadex and Concanavalin A affinity column chromatography. The purified enzyme has a high specific enzyme activity and is free from any extraneous proteins judging from immunochemical criteria and biochemical criteria such as SDS-polyacrylamide gel electrophoresis. The purified enyzme produced a monospecific anti-PAP antisera in animals and this anti-PAP antibody did not cross-react with other human acid phosphatases.

Acid Phosphatase↗
PubMed1978

Human prostatic acid phosphatases: II. A double--antibody radioimmunoassay.

A double-antibody radioimmunoassay method for prostate-specific acid phosphatase (PAP) is presented. Experimental details are outlined to assess the reproducibility and reliability of the method under assay conditions. The upper limit of the serum PAP levels in the present assay was set at 2.4 ng/100 microliter by 162 determinations of normal serum samples. The serum PAP levels of patients with nonprostatic malignant tumors fell in the normal range, whereas the levels higher than 4.0 ng/100 microliter were found in patients with prostatic carcinoma.

Acid Phosphatase↗
PubMed1978

Human prostatic acid phosphatases: III. Counterimmunoelectrophoresis for rapid identification.

When serial dilution of standard prostatic acid phosphatases (PAP) was reacted with constant amounts of anti-PAP serum by counterimmunoelectrophoresis (CIEP), the detection end point of enzyme concentration was 0.25 ng in a 10 microliter sample volume. The PAP concentrations in unknowns can be quantitated by comparing the dilution end points of reference PAP with the testing samples. Serum PAP levels were determined by a radioimmunoassay (RIA) and CIEP using normal male and female sera and serum samples from patients with prostatic cancer and nonprostatic tumors. An excellent correlation was observed between the two assay results. According to RIA data, the concentration of PAP higher than 0.4 ng per 10 microliter (or 4.0 ng per 100 microliter) signify the elevation of serum or bone marrow PAP level beyond normal range (normal value 1.6 +/- 0.8 ng/100 microliter). Thus, the CIEP assay will be a simple and reliable screening method for the serum PAP levels in the clinical diagnosis of prostatic cancer.

Acid Phosphatase↗