Detection Of Prostatic Acid Phosphatase Research Articles

A simple assay for direct colorimetric detection of prostatic acid phosphatase (PAP) at fg levels using biphosphonated loaded PEGylated gold nanoparticles

A fast and sensitive colorimetric assay for the determination of prostatic acid phosphatase (PAP) levels using biphosphonates-PEG-coated gold nanoparticles (BP-PEG-AuNPs) has been developed. Addition of different amounts of PAP to the AuNPs results in a significant change of color, from a red-wine color to purple, and finally to blue. The PAP should bind onto the AuNPs surface and crosslink the AuNPs inducing their aggregation and as a consequence a color change of the solution from wine red to purple/blue. The color change was monitored by UV–vis spectrophotometry or with the naked eye. The ensuing concentration-dependent red-shift of surface plasmon resonance absorption allows the determination concentration within the fg range in 10 min. Importantly, the visual detection limit (1 ng/mL) allows the rapid differential diagnosis with naked eye or image analyzer. This demonstrates that the color modification observed with BP-PEG-AuNP is effectively due to an interaction between PAP and BP.

Detection of antibodies to human immunodeficiency virus in vaginal secretions by immunoglobulin G antibody capture enzyme-linked immunosorbent assay: application to detection of seminal antibodies after sexual intercourse.

In order to evaluate a commercial immunoglobulin G (IgG) antibody capture enzyme-linked immunoassay (ELISA) (Wellcozyme HIV1 + 2 Gacelisa; Murex Diagnostics Limited, Dartford, United Kingdom) for the detection of antibodies to human immunodeficiency virus (HIV) in vaginal secretion samples (VS) from HIV-seropositive and -seronegative women, serum samples (S) and VS were obtained from 129 African women living in the Central African Republic, a country of high HIV prevalence. Sera were tested for HIV by routine second-generation ELISA with confirmatory Western blot (immunoblot) (WB). By the Gacelisa IgG immuno-capture assay, 45 VS were positive and 84 were negative, whereas by WB, 44 VS were confirmed positive and 85 were confirmed negative. Considering WB as a reference, the IgG immunocapture assay in VS was 97.7% sensitive (43 of 44 positive samples) and 97.6% specific (83 of 85 negative samples). Of 42 HIV-seropositive women, 41 (97.6%) had S and VS that both were HIV positive (S+ VS+), and of 87 HIV-seronegative women, 83 (95.4%) had S and VS that both were HIV negative (S- VS-). Five women had discordant results for S and VS. One (S+ VS-) possibly had a false-negative VS result. Two (S- VS+) had similar indeterminate patterns for S and VS in WB. Two (S- VS+) had a typical HIV-positive pattern on WB of VS, whereas S results in WB were indeterminate in one case and negative in the other case; for both women, detection of prostatic acid-phosphatase was positive in VS, strongly suggesting recent sexual intercourse with an HIV-positive man. Because all HIV-infected men have detectable IgG antibodies to HIV in the seminal fluid, an HIV-seronegative rape victim with HIV-positive VS (S- VS+) should receive short-term antiviral therapy to prevent possible HIV transmission.

Improved immunohistochemical detection of prostatic acid phosphatase by a monoclonal antibody

A monoclonal antibody with high affinity to acid phosphatase isoenzyme 2 (Ab-AcP2) was selected to examine its binding to different normal and tumor tissues using the indirect immunohistochemical method. Both mature prostatic epithelial cells in the prostate and the highly dedifferentiated prostatic cancer cells in the bone marrow showed strong binding to the antibody. Among nonprostatic tissues, only bone marrow, breast, and kidney showed trace staining in some specimens. The specificity of Ab-AcP2 was much better than that of the polyclonal antibody to acid phospatase previously reported. When the antibody to the prostate-specific antigen (Ab-PSA) was used, weak background staining was often encountered, and weak to moderate stains were seen in the prostatic stroma, bone marrow, lung, skin, and melanoma.

A comparative study of the use of monoclonal antibodies using three different immunohistochemical methods: an evaluation of monoclonal and polyclonal antibodies against human prostatic acid phosphatase.

The use of immunohistochemical methods has been advocated for the detection and localization of prostatic acid phosphatase in paraffin sections of human prostate. This article explores the possible advantages of utilizing monoclonal antibodies in this method. Monoclonal antibodies, specific for human prostatic acid phosphatase, were integrated into three different immunohistochemical procedures. In the first method, a three-layer peroxidase-antiperoxidase (PAP) system was employed; the monoclonal antibody was followed by rabbit bridge antibody directed against mouse immunoglobulin and mouse PAP complex. The second method was a three-layer system utilizing biotin-labeled horse anti-mouse antibody as "bridge" antiserum between the primary monoclonal antibody and an avidin-biotin-horseradish peroxidase complex. The third method was a four-layer system; the monoclonal antibody was followed by rabbit anti-mouse serum, swine anti-rabbit immunoglobulin as the bridge antibody and rabbit PAP complex. It was found that some, but not all, monoclonal antibodies can be used for the detection of prostatic acid phosphatase in paraffin sections. The four-layer PAP method was found to be the most sensitive method of the three systems tested; however, the avidin-biotin method required the least amount of time. No significant difference in the quality of staining was observed between monoclonal antibodies and carefully absorbed conventional antiserum.

The Detection of Prostatic Acid Phosphatase in Vaginal Swabs by Radioimmunoassay

A commercial radioimmunoassay (RIA) kit was compared with two other routine methods for the confirmation of the presence of prostatic acid phosphatase (PAP) in post-coital vaginal swabs. Swabs were collected, by 4 donors, at various times after sexual intercourse. The length of time after intercourse that PAP was detected in the vagina varied considerably between individuals.

The immunohistochemical detection of prostatic acid phosphatase: its possibilities and limitations in tumour histochemistry.

The immunological specificity of the Amsterdam rabbit antiserum against human prostatic acid phosphatase was studied on paraffin sections of 200 prostatic carcinomas and 330 control tissues using an indirect peroxidase technique. Peripheral blood leucocyte smears were also investigated with a fluorescent technique. In a limited number of cases, the mixed aggregation immunocytochemical method was also applied as post-primary incubation procedure. The diaminobenzidine (DAB) final reaction product of the peroxidase technique, carried out under standard conditions, was quantified in some cases using the Leyden Television Analysis System (LEYTAS) with a built-in standard. A positive reaction was obtained in 96.5% of the prostatic carcinomas. Only 2.1% of the non-prostatic tumour cases (23 types) showed a positive reaction, namely six out of 10 insulomas and one out of 10 carcinoid tumours. The beta-cells of the normal islet of Langerhans and the leucocytes in the smears showed a positive reaction. The sensitivity of the peroxidase method, judged subjectively, is not only dependent on the circumstances of fixation, embedding and incubation but also on the degree of tumour differentiation. None of the three prostatic carcinomas studied reached the level of DAB staining intensity shown by the hyperplastic prostatic epithelium.

Immunologic detection of prostatic acid phosphatase: Critique II

Immunologic detection of prostatic acid phosphatase: Critique II

Immunologic detection of prostatic acid phosphatase: Critique I

Immunologic detection of prostatic acid phosphatase: Critique I

Counter immunoelectrophoresis for detection of human prostatic acid phosphatase

An immunochemical method f or detection of prostatic acid phosphatase is described. Acid phosphatase was obtained from benign human prostatic tissue. A specific antiserum to this enzyme was produced in rabbits. A counter immunoelectrophoretic method utilizing the specific antiserum with a chemical staining technique has been developed. Clinical trials have indicated the usefulness of this method for the specific determination of prostatic acid phosphatase.

Comparison of human prostatic acid phosphatase by measurement of enzymatic activity and by radioimmunoassay.

We compared results of measurement of prostatic acid phosphatase activity in serum and various tissues by enzymatic assay and radioimmunoassay. By enzymatic assay, activity in serum is lost rapidly, even at room temperature. In contrast, there was no change in antigenic activity during 48 h by radioimmunoassay. The radioimmunoassay was more specific in 12 tissues and in serum than were several enzymatic assays that make use of inhibitors of the enzyme. The enzymatic assay resulted in 26.6% (24/90) false positives from non-prostatic cancer patients. In contrast, with radioimmunoassay there were only 5.5% (5/90) false positives. We conclude that immunological detection of prostatic acid phosphatase is the more reliable technique.

Spermine and Choline Identification by Thin-Layer Chromatography

Various methods are available for the detection of prostatic acid phosphatase [1, 2], spermine, choline [3], and spermatozoa. Aspermatic seminal stains are increasing in number due to vasectomies. In these cases location of spermatozoa is not possible. Difficulties are also frequently encountered in the location of spermatozoa even when present in dried seminal stains. This paper sets forth a practical, rapid, inexpensive, and sensitive thin-layer chromatographic method for the detection of spermine and choline. No interferences have been noted from blood, vaginal secretions, saliva, douche powders, urine, or the azo dye (Fast Blue B) for the detection of prostatic acid phosphatase.

The Detection of Prostatic Acid Phosphatase by Antibody Reactions in Gel Diffusion

Summary Prostatic acid phosphatase was demonstrated in electrophoretic patterns of prostatic fluid in the region corresponding to the serum α2- and β-globulins. In gel diffusion precipitation, this enzymatic activity was localized in two distinct bands of dense brown, speckled appearance. The titration end point of the major band varied with the sample of prostatic fluid; some were as high as 1:16000. In immunoelectrophoresis, the activity was again localized in two of the precipitin bands that were formed with the homologous antiserum. These bands were clearly of different electrophoretic mobility, suggesting that there are two different molecules having similar enzymatic properties. A number of organ extracts were tested for this phosphatase activity, namely, seminal vesicle, kidney, testicle, liver, lung and prostate gland. All of these were negative except for prostate extract, which did show one line of reaction. Normal serum was also negative. Serum from patients with carcinoma of the prostate were also positive, but only in some of the experiments. This is being further studied.

Detection of prostatic acid phosphatase in serum by tartrate inactivation technic.

Detection of Prostatic Acid Phosphatase in Serum by Tartrate Inactivation Technic Get access E. H. Bensley, M.D., E. H. Bensley, M.D. Department of Metabolism and the McGill University Clinic, The Montreal General Hospital, Montreal, Canada Search for other works by this author on: Oxford Academic Google Scholar Audrey Drysdale, B.Sc., Audrey Drysdale, B.Sc. Department of Metabolism and the McGill University Clinic, The Montreal General Hospital, Montreal, Canada Search for other works by this author on: Oxford Academic Google Scholar Ruth Osiek, M.Sc. Ruth Osiek, M.Sc. Department of Metabolism and the McGill University Clinic, The Montreal General Hospital, Montreal, Canada Search for other works by this author on: Oxford Academic Google Scholar American Journal of Clinical Pathology, Volume 26, Issue 3, 1 March 1956, Pages 247–249, https://doi.org/10.1093/ajcp/26.3.247 Published: 01 March 1956 Article history Received: 06 October 1955 Revision received: 15 December 1955 Accepted: 16 December 1955 Published: 01 March 1956