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At least 631 records · Page 35Linked to original sources
PubMed1978

Expression of human prostatic acid phosphatase in a pancreatic islet cell carcinoma.

The immunologic specificity of human prostatic acidphosphatase has been established by several previous investigations as well as in this study. An apparent exception to this specificity was observed--a case of pancreatic islet cell carcinoma metastasized to the liver produced acid phosphatase that was immunologically indistinguishable from the prostatic acid phosphatase. In this case, the possibility of prostatic involvement was convincingly ruled out by clinical follow-ups and by postmortem pathologic studies. Highly purified prostatic acid phosphatase and this tumor acid phosphatase exhibited very similar Km values and identical molecular weights. Immunochemical analysis of the two enzymes using antiprostatic acid phosphatase sera showed that enzymes are antigenically identical. The implications of our observation are discussed in relation to clinical application of immunoassays for prostatic phosphatase in the future and to the molecular basis of human acid phosphatase polymorphism.

Acid Phosphatase↗
PubMed1975

Molecular properties of multiple forms of acid phosphatase from horse liver.

1. Horse liver acid phosphatase was separated into two partially purified fractions differing in molecular weight (enzyme I about 100 00, enzyme II about 25 000). 2. Enzyme I was separated into several subfractions by DEAE-cellulose chromatography and isoelectric focusing. 3. Molecular weight, sedimentation coefficient and effective molecular radii were determined for acid phosphatases I and II by gel filtration and density-gradient centrifugation.

Acid Phosphatase↗
PubMed1977

Seminal fructose and acid phosphatase in vasectomised men.

Seminal fructose and acid phosphatase levels have been determined in 30 vasectomised and 30 nonvasectomised healthy adults, both the groups being closely matched for age (32 to 45 years). The fructose and acid phosphatase values in the vasectomised men, 3 to 6 months after the operation, were 316 +/- 36 mg% and 2,098 +/- 112 K.A. units/ml, respectively, while in the control group they were 251 +/- 28 mg% and 1,932 +/- 92 K.A. units/ml. The differences are statistically significant (P less than 0.001) and the possible implications of the post-vasectomy rise in these androgen dependent seminal constituents are discussed.

Acid Phosphatase↗
PubMed2003

Tissue-specific expression of the prostatic acid phosphatase promoter constructs.

Human prostatic acid phosphatase (hPAP) is intensely expressed in epithelial cells of the prostate gland following puberty. Its regulatory regions were analyzed in transgenic mice and cell line transfections, in order to clarify the mechanisms of tissue-specific gene expression. A construct containing the sequence of hPAP between the nucleotides -734 and +467 in front of the CAT reporter gene was significantly expressed in the prostate of transgenic mice, while the proximal promoter -734/+50 alone achieved low levels of CAT mRNA in all tissues analyzed. Five homologous sequences (A-E) for our previously identified prostatic GAAAATATGATA DNA-binding site were found in the area. The competitive reactions in electrophoretic mobility shift assays suggested that the same nuclear factor binds to the GAAAATATGATA and the sites C and E. The importance of the intronic area +57/+467 on the androgen-activated expression in prostatic cells was shown by the reporter construct containing heterologous promoter.

Acid Phosphatase↗
PubMed1986

Seminal acid phosphatase in relation to fertility.

In a study involving 176 males attending an infertility clinic and 88 controls awaiting elective vasectomy, the semen acid phosphatase activity was found to be significantly higher in the former group (p less than 0.001). However, no definite relationship of semen acid phosphatase level to ejaculate volume, sperm motility, viability, morphology, seminal zinc, magnesium or fructose was observed in either group. The distribution of acid phosphatase in the males attending the infertility clinic, unlike that of the controls, was found to be bimodal. 32 presumably infertile males had acid phosphatase values exceeding the control mean +/- 2 SD. These 32 nevertheless did not have a significantly different mean ejaculate volume, sperm motility, morphology or viability, when compared with the group with normal acid phosphatase levels. Causes of the bimodal distribution of concentrations of acid phosphatase are discussed.

Acid Phosphatase↗
PubMed1985

Assessment of serum radioimmune and enzymatic prostatic acid phosphatase and radioimmune creatine kinase BB for monitoring response to therapy in metastatic prostatic carcinoma.

Objective documentation of tumor response in patients with metastatic prostatic cancer is difficult. To evaluate a radioimmunoassay for creatine kinase BB, two commercial radioimmunoassays for prostatic acid phosphatase, and an enzymatic acid phosphatase measurement in monitoring the status of advanced prostatic carcinoma, we assayed sera from 34 patients with Stage D-2 disease prior to and during systemic treatment with combination chemotherapy or hormonal manipulation. Prior to treatment, the creatine kinase BB level was elevated less often (48%) than all three assays for acid phosphatase (83 to 91%). During therapy, all four test results both increased and decreased whether the patients were responding to or progressing on therapy. Test results usually declined when patients had documented responses to therapy, particularly when hormonal therapy was used. However, when patients progressed on therapy, test results also declined at least as often as they increased. No test was consistent enough to serve as a sole indication of tumor response. The three acid phosphatase assays performed similarly, with no evident advantage of radioimmunoassay over the enzymatic assay. Creatine kinase BB was generally inferior to all three acid phosphatase assays.

Acid Phosphatase↗
PubMed1986

Human prostatic acid phosphatase has phosphotyrosyl protein phosphatase activity.

The major secreted isoenzyme of human prostatic acid phosphatase (PAcP) (EC 3.1.3.2), which catalyses p-nitrophenyl phosphate (PNPP) hydrolysis at acid pH values, was found to have phosphotyrosyl protein phosphatase activity since it dephosphorylated three different phosphotyrosine-containing protein substrates. Several lines of evidence are presented to show that the phosphotyrosyl phosphatase and PAcP are the same enzyme. A highly purified PAcP enzyme preparation which contains a single N-terminal peptide sequence was used to test for the phosphotyrosyl phosphatase activity. Both activities comigrated during gel filtration by high performance liquid chromatography. Phosphotyrosyl phosphatase activity and PNPP acid phosphatase activity exhibited similar sensitivities to different effectors. Both phosphatase activities showed the same thermal stability. Specific anti-PAcP antibody reacted to the same extent with both phosphatase activities. PNPP acid phosphatase activity was competitively inhibited by the phosphotyrosyl phosphatase substrate. To characterize further the phosphotyrosyl phosphatase activity, the Km values using different phosphoprotein substrates were determined. The apparent Km values for phosphorylated angiotensin II, anti-pp60src immunoglobulin G and casein were in the nM range for phosphotyrosine residues, which was about 50-fold lower than the Km for phosphoserine residues in casein.

Acid Phosphatase↗
PubMed1978

Counterimmunoelectrophoresis in determination of prostatic acid phosphatase in human serum.

We evaluated counterimmunoelectrophoresis for use in measuring prostatic acid phosphatase in detection of prostatic cancer. After staining for acid phosphatase, we could detect as little as 0.3 ng of purified enzyme standard complexed with antibody by this technique. However, when serum samples were used as antigen, the method was less sensitive (1.5-2.0 ng) because some of the serum proteins migrate with the phosphatase and decrease the intensity of the stain for acid phosphatase. For this reason we could not detect the phosphatase in serum samples of normal persons; only patients with moderately (or greater) increased activity in their serum showed positive results. In contrast, by radioimmunoassay as little as 1.0 ng of the phosphatase can be detected in serum.

Acid Phosphatase↗
PubMed1982

Prostatic acid phosphatase, purification and iodination using Iodogen.

Prostatic acid phosphatase was purified from prostatic adenomas. The procedure involved chromatography on Concanavalin A-Sepharose, DEAE-cellulose, Bio-Gel P-150 and L-tartrate-Sepharose. The purified phosphatase hydrolyzed p-nitrophenyl phosphate at a rate of 270 mumol . mg-1 . min-1 (25 degrees C) and showed homogeneity upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The final prostatic acid phosphatase preparation was pure and the antisera were monospecific as judged by the highly sensitive technique of crossed immunoelectrophoresis. Of the procedures evaluated for the iodination of the purified enzyme, oxidation with Iodogen was found to give the best iodinated product.

Acid Phosphatase↗
PubMed1982

Polymorphism of serum acid phosphatase in the rat.

Polymorphism of serum acid phosphatase was detected by electrofocusing in acrylamide gel. The locus has two alleles Apsa and Apsb that segregated in the backcross progeny (A x B) F1 x B in a 1:1 ratio. The phenotype APS-A is dominant in the F1 generation. The gene for serum acid phosphatase segregated independently of the major histocompatibility complex and of the sex of the rats.

Acid Phosphatase↗
PubMed1993

Purification and partial characterization of acid phosphatase from Candida lipolytica.

Non-specific acid phosphatase from Candida lipolytica cells was purified 111-fold by chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 and Sepharose 4B. The enzyme is a glycoprotein containing 67% neutral sugars. The molecular mass of the highly purified acid phosphatase was found to be approximately 95 kDa by both SDS-PAGE and gel filtration. The pH and temperature optima were 5.8 and 55 degrees C, respectively. The enzyme was stable at pH values between 3.5 and 5.5 and at temperatures up to 60 degrees C. The purified phosphatase had a Km value of 3.64 mM for p-nitrophenyl phosphate and showed broad substrate specificity.

Acid Phosphatase↗
PubMed1998

Is acid phosphatase activity present in bone matrix at sites of endochondral ossification in rabbit fracture callus?

It has been suggested that acid phosphatase activity is present in newly formed bone matrix at sites of endochondral ossification in rabbit fracture calluses. Because acid phosphatases are usually found intracellularly, it was decided to test this possibility more rigorously. Tissue from 10- and 14-day healing rabbit fractures was subjected to a series of critical tests for acid phosphatases with a pH optimum of 5.0. Fluoride, tartrate and molybdate were used as potential inhibitors of acid phosphatase activity. The effects of several counterstaining protocols were also investigated. A fluoride- and tartrate-resistant acid phosphatase is located in osteoclasts and mononuclear phagocytes. Diffuse staining of the bone matrix is seen, but it is dependent upon the length of incubation in the substrate medium and the distance from the acid phosphatase-reacting cells. It is concluded that the coloration of the bone matrix is probably caused by diffusion of the dye and reaction product and is, therefore, artifactual.

Acid Phosphatase↗
PubMed1993

Purification and properties of the native form of the purple acid phosphatase from bovine spleen.

The purple acid phosphatase (PAP) from bovine spleen has been shown to exist as a single ca. 36-kDa polypeptide in intact spleen tissue. The previously isolated microheterogeneous complex of 15-kDa and 23- or 21-kDa subunits appears to arise from proteolytic cleavage of an exposed, highly variable loop in the polypeptide chain. Small amounts of a single polypeptide form, presumed to be the native form of the enzyme, have been obtained; this has permitted its optical and EPR spectra and fundamental kinetic properties to be determined. The most notable difference between the native and two-subunit forms of PAP is a ca. 3-fold higher enzymatic activity for the latter, which is due to a simple increase in Vmax. The two forms are very similar spectroscopically and chemically and appear to differ only in the loss of a highly antigenic ca. five amino acid segment of the polypeptide between positions 155 and 160 but not in NH2-terminal sequence or in carbohydrate content. Analysis of published sequence data suggests that the existence of an exposed highly antigenic loop at positions corresponding to 155-161 of the spleen PAP sequence is a relatively general feature of PAP's. Trypsin and chymotrypsin cleave both bovine spleen PAP and uteroferrin, apparently in this region, with significant enhancement of enzymatic activity.

Acid Phosphatase↗
PubMed1979

Phosphonic and arsonic acids as inhibitors of human red cell acid phosphatase and their use in affinity chromatography.

1. In order to obtain an effective ligand for affinity chromatography of the low molecular weight acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) from human red cells nine phosphonic and two arsonic acid substrate analogues were investigated as potential inhibitors. The two forms of acid phosphatase type B (b1 and b2) were isolated and partially purified using conventional methods and the inhibitory action of the substrate analogs investigated. 2. Four of the phosphonic acids were relatively effective competitive inhibitors. It appears that certain structural and electronic requirements have to be fulfilled by the phosphonic acids in order to exhibit significant affinity for the enzyme. A high affinity appears to require the presence of a bulky, hydrophobic moiety which has to be separated from the phosphorus atom by the distance of one atom. 3. p-Aminobenzylphosphonic acid exerted the highest affinity for acid phosphatase with a pH optimum at 6.5. Ki values of 4 . 10(-4) and 6 . 10(-4) M were found for the b1 and b2 forms, respectively. 4. Coupling of p-aminobenzylphosphonic acid to Agarose yielded an effective and specific affinity medium. By means of affinity chromatography using this medium, acid phosphatase was purified 500-fold in a single step.

Acid Phosphatase↗
PubMed1975

Distribution of acid phosphatase, beta-glucuronidase, n-acetyl-beta-d-glucosaminidase and beta-galactosidase in cornea of albino rabbit.

Activities of acid phosphatase, beta-glucuronidase, N-acethyl-beta-D-glucosaminidase and acid beta-galactosidase were investigated histochemically in rabbit corneas. Frozen sections after block fixation in cold 4% formaldehyde with 1% CaCl2 followed by washing in cold physiological saline as well as cold microtome sections of corneas quenched in petroleter chilled with acetone-dry ice mixture, transferred to nonprecooled slides or semipermeable membranes were used. Standard aqueous media were employed in the case of free-floating frozen sections of fixed corneas as well as of cold mictrotome sections (postfixed in cold 4% formaldehyde). Agar media were used in connection with the technic of semipermeable membranes. Gomori method (in the case of acid phosphatase), simultaneous azocoupling methods (substrates derivated of naphthol-AS-BI with hexazonium-p-rosanilin) in the case of acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase and the indigogenic method in the case of acid beta-galactosidase were applied. Enzyme activities in sections of fixed corneas were minimal in comparison with those in cold microtome sections of unfixed material revealed particularly with the technic of semipermeable membranes which is to be preferred. This technic is recommended in studies concerned with lysosomal enzymes in the cornea, particularly in keratocytes. All enzymes investigated were present in corneal epithelium, keratocytes and endothelium. Acid phosphatase displayed the highest activity followed by beta-glucuronidase and acetyl-beta-D-glucosaminidase. The activity of beta-galactosidase was the lowest. For the demonstration of activities in keratocytes sections parallel to the surface are very suitable. In these sections enzyme activities were demonstrated in small granules (apparently lysosomes) present in the central part of their cytoplasm as well as in projections. Diffuse staining was also seen, being the highest in the case of acid phosphatase.

Acetylglucosaminidase↗
PubMed1987

The purification of acid phosphatase from honey bee venom (Apis mellifica).

Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.

Acid Phosphatase↗
PubMed1980

Antigenic and molecular relationship of human prostatic acid phosphatase isoenzymes.

Human prostate contains two major acid phosphatase isoenzymes, 2 and 4. Isoenzyme 2 is a glycoprotein with slow electrophoretic mobility. Treatment with sialidase increases its electrophoretic mobility to approach that of isoenzyme 4 which contains no carbohydrate. The identical protein structure of isoenzyme 2 and 4 was revealed by their antigenic identity. Serum acid phosphatase isoenzyme 5 is a different protein species and has no antigenic relationship to isoenzymes 2 and 4. Our results indicate that the elevation of isoenzyme 5 in late stages of prostatic carcinoma with bone metastases is attributable to increased osteoclastic activity.

Acid Phosphatase↗