scholarly journals A Substitute Presumptive Test for Screening of Semen using Sodium –p– Nitrophenyl Phosphate (NaPNPP)

2021 ◽  
Author(s):  
Daniel Njau ◽  
Accadius Lunayo ◽  
Johansen Odour
Keyword(s):  
Acid Phosphatase ◽  
Sexual Assault ◽  
Seminal Fluid ◽  
Preliminary Test ◽  
Crime Scene ◽  
Test Methods ◽  
Spectrophotometric Analysis ◽  
Simple Method ◽  
Fluid Identification ◽  
Nitrophenyl Phosphate

Abstract BackgroundIn forensic investigation of alleged sexual crimes, presumptive semen detection test methods are commonly used to reach preliminary identification of seminal fluid in questioned samples. These methods are based on the detection of components of semen such as enzyme acid phosphatase (AP). Of these methods, the acid phosphatase identification method still remains the most reliable and widely used presumptive test due to high activity of the AP in seminal fluid. In standard AP test, Bretamine Fast Blue B (FBB) reagent is used. However FBB has been explicitly classified as carcinogenic. Although FBB has been handled safely over time, there is a need at the moment to develop a simple, readily available, reliable and efficient method for screening the presence of semen in any material collected as evidence in a sexual assault crime.Given the improved sensitivity of DNA profiling tests that have been introduced in to routine forensic casework over recent years, the need for improved sensitivity at this first stage of detection has never been higher. FindingsHere we highlight a simple method using readily available reagents in standard biochemical laboratory as a substitute for the standard AP test for seminal fluid identification from a crime scene. This method is based on the hydrolysis of sodium–p-nitrophenyl phosphate at pH 5.5 by the acid phosphatase to produce an intense yellow coloured complex in 15 seconds. ConclusionsThe method presented is sensitive, reliable, efficient and routinely used in standard biochemical and pathology laboratories for spectrophotometric analysis of alkaline phosphatase. It can be easily and readily applied as a preliminary test for identification of semen at a crime scene that involves sexual assault.

A Preliminary Investigation Using p-Nitrophenyl Phosphate to Quantitate Acid Phosphatase on Swabs Examined in Cases of Sexual Assault

1978 ◽  
Vol 18 (3) ◽  
pp. 174-178 ◽  
Author(s):  
Anne Davies
Keyword(s):  
Acid Phosphatase ◽  
Sexual Assault ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Seminal Fluid ◽  
Preliminary Investigation ◽  
Cotton Wool ◽  
Nitrophenyl Phosphate

A method for determining the level of acid phosphatase activity of material on cotton-wool swabs, used by police surgeons in cases of sexual assault, has been described. The results showed that it was particularly useful as an indication of the presence of seminal fluid in the absence of spermatozoa.

Presumptive Screening Test for Seminal Acid Phosphatase Using Sodium Thymolphthalein Monophosphate

1983 ◽  
Vol 66 (1) ◽  
pp. 207-209
Author(s):  
Howard Seiden ◽  
George T Duncan
Keyword(s):  
Acid Phosphatase ◽  
Sexual Assault ◽  
Screening Test ◽  
Seminal Fluid ◽  
Health Hazard ◽  
Effective Alternative ◽  
Potential Health ◽  
Fluid Analysis ◽  
Potential Health Hazard ◽  
High Degree

Abstract The use of sodium thymolphthalein monophosphate for presumptive seminal acid phosphatase testing is discussed. Recent evidence reveals that the dye (o-dianisidine) used in conjunction with α-naphthyl phosphate for seminal acid phosphatase testing is a carcinogenic hazard. Numerous tests for seminal acid phosphatase were conducted with swabs from sexual assault kits to compare both substrates. Results of tests using sodium thymolphthalein or α-naphthyl phosphate correlated exactly. Sodium thymolphthalein is an effective alternative for preliminary seminal fluid analysis because of its high degree of selectivity and stability, and because it eliminates the potential health hazard.

Acid phosphatase activity of six ectomycorrhizal fungi

1979 ◽  
Vol 57 (11) ◽  
pp. 1203-1205 ◽  
Author(s):  
Iwan Ho ◽  
Bratislav Zak
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Test Methods ◽  
Starch Gel Electrophoresis ◽  
Tree Roots ◽  
Nitrophenyl Phosphate ◽  
Starch Gel

Six ectomycorrhizal fungi commonly associated with Douglas-fir were tested in vitro for acid phosphatase activity by measuring the amount of p-nitrophenyl phosphate converted to p-nitrophenol and by examining their production of isoenzymes detectable by starch gel electrophoresis. Both test methods showed acid phosphatase activity to be highest in Hebeloma crustuliniforme, followed by progressively lower activity in Laccaria laccata, Amanita muscaria, and Thelephora terrestris. Rhizopogon vinicolor and Piloderma bicolor showed low activity. We discuss the significance of these fungi in the utilization of complex phosphates by tree roots.

Further Information on the Use of p-Nitrophenyl Phosphate to Quantitate Acid Phosphatase on Vaginal Swabs Examined in Cases of Sexual Assault

1979 ◽  
Vol 19 (3) ◽  
pp. 170-172 ◽  
Author(s):  
Julie Allard ◽  
Anne Davies
Keyword(s):  
Acid Phosphatase ◽  
Sexual Assault ◽  
Sexual Intercourse ◽  
Time Interval ◽  
Clear Indication ◽  
Simple Test ◽  
Nitrophenyl Phosphate ◽  
Vaginal Swabs

A simple test for screening swabs for the presence of semen has now been used on over 1000 vaginal swabs. The preliminary conclusions reached in a previous paper (Davies, 1978) are discussed and these have subsequently been shown to be correct: however, more information is now available. Despite the limitations of the method, the results can give a clear indication of the presence of semen. The test also continues to be of use on some occasions when the time interval between sexual intercourse and the swab being taken is contentious. Some modifications to the method arc also described.

scholarly journals Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate

2015 ◽  
Vol 71 (2) ◽  
pp. 199-205 ◽  
Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Phosphatase Activity ◽  
Small Molecule ◽  
Molecular Basis ◽  
Protein Tyrosine Phosphatases ◽  
Simple Method ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Nitrophenyl Phosphate

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.

Detection of prostatic tissue and seminal plasma peptides reacting with human seminal fluid acid phosphatase antibodies

1986 ◽  
Vol 18 (11) ◽  
pp. 1005-1013 ◽  
Author(s):  
Radosława Kuciel ◽  
Izydor Apostoł ◽  
Ewa Wasylewska ◽  
Włodzimierz S. Ostrowski ◽  
Iga Steuden ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Seminal Plasma ◽  
Seminal Fluid ◽  
Prostatic Tissue

scholarly journals Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture

1972 ◽  
Vol 127 (1) ◽  
pp. 87-96 ◽  
Author(s):  
P. G. Bolton ◽  
A. C. R. Dean
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Continuous Culture ◽  
Activity Profile ◽  
Glucose Effect ◽  
Ph Values ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Phosphatase synthesis was studied in Klebsiella aerogenes grown in a wide range of continuous-culture systems. 2. Maximum acid phosphatase synthesis was associated with nutrient-limited, particularly carbohydrate-limited, growth at a relatively low rate, glucose-limited cells exhibiting the highest activity. Compared with glucose as the carbon-limiting growth material, other sugars not only altered the activity but also changed the pH–activity profile of the enzyme(s). 3. The affinity of the acid phosphatase in glucose-limited cells towards p-nitrophenyl phosphate (Km 0.25–0.43mm) was similar to that of staphylococcal acid phosphatase but was ten times greater than that of the Escherichia coli enzyme. 4. PO43−-limitation derepressed alkaline phosphatase synthesis but the amounts of activity were largely independent of the carbon source used for growth. 5. The enzymes were further differentiated by the effect of adding inhibitors (F−, PO43−) and sugars to the reaction mixture during the assays. In particular, it was shown that adding glucose, but not other sugars, stimulated the rate of hydrolysis of p-nitrophenyl phosphate by the acid phosphatase in carbohydrate-limited cells at low pH values (<4.6) but inhibited it at high pH values (>4.6). Alkaline phosphatase activity was unaffected. 6. The function of phosphatases in general is discussed and possible mechanisms for the glucose effect are outlined.

scholarly journals [Phosphotyrosine]protein phosphatase in rat brain. A major [phosphotyrosine]protein phosphatase is a 23 kDa protein distinct from acid phosphatase

1986 ◽  
Vol 239 (1) ◽  
pp. 155-162 ◽  
Author(s):  
M Okada ◽  
K Owada ◽  
H Nakagawa
Keyword(s):  
Acid Phosphatase ◽  
Molecular Mass ◽  
Rat Brain ◽  
Column Chromatography ◽  
Protein Phosphatase ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Sodium Vanadate ◽  
Nitrophenyl Phosphate ◽  
Phosphotyrosine Protein Phosphatase

A [phosphotyrosine]protein phosphatase (PTPPase) was purified almost to homogeneity from rat brain, with [32P]p130gag-fps, an oncogene product of Fujinami sarcoma virus, as substrate. The characteristics of the purified preparation of PTPPase were as follows: the enzyme was a monomer with a molecular mass of 23 kDa; its optimum pH was 5.0-5.5; its activity was not dependent on bivalent cations; its activity was strongly inhibited by sodium vanadate, but was not inhibited by ZnCl2, L(+)-tartrate or NaF; it catalysed the dephosphorylation of [32P]p130gag-fps, [[32P]Tyr]casein, p-nitrophenyl phosphate and L-phosphotyrosine, but did not hydrolyse [[32P]Ser]tubulin, L-phosphoserine, DL-phosphothreonine, 5′-AMP, 2′-AMP or beta-glycerophosphate significantly. During the purification, most of the PTPPase activity was recovered in distinct fractions from those of conventional low-molecular-mass acid phosphatase (APase), which was reported to be a major PTPPase [Chernoff & Li (1985) Arch. Biochem. Biophys. 240, 135-145], from DE-52 DEAE-cellulose column chromatography, and those two enzymes could be completely separated by Sephadex G-75 column chromatography. APase also showed PTPPase activity with [32P]p130gag-fps, but the specific activity was lower than that of PTPPase with molecular mass of 23 kDa, and it was not sensitive to sodium vanadate. These findings suggested that PTPPase (23 kDa) was the major and specific PTPPase in the cell.

Development of a stable reference material for prostatic acid phosphatase.

1984 ◽  
Vol 30 (8) ◽  
pp. 1327-1331 ◽  
Author(s):  
P H Duncan ◽  
R L Van Etten ◽  
M L MacNeil ◽  
L M Shaw
Keyword(s):  
Catalytic Activity ◽  
Acid Phosphatase ◽  
Reference Material ◽  
Sodium Acetate ◽  
Seminal Fluid ◽  
Reference Method ◽  
Prostatic Acid Phosphatase ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Abstract We describe the development of a stable reference material for prostatic acid phosphatase, derived from human prostatic tissue and human seminal fluid. The enzyme was purified by an L-tartramic acid affinity-chromatography technique. Two-dimensional electrophoresis revealed essentially no contaminating proteins, and specific tests revealed no contaminating enzymes. The preparations, in a matrix containing 30 g of human serum albumin and 0.1 mol of sodium acetate per liter, pH 6.0, were studied with respect to stability of both catalytic activity and immunological identity. We conclude that the preparations from either source are satisfactorily stable, and that either is acceptable for use in preparing clinical reference materials. These materials will be used in developing a reference method.

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