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At least 865 records · Page 48Linked to original sources
PubMed1980

Rate of decrease of glutamyltransferase and acid phosphatase activities in the human vagina after coitus.

I studied the rate at which gamma-glutamyltransferase (EC 2.3.2.2) and acid phosphatase (EC 3.1.3.2) activities decrease in the healthy human vagina after coitus. Specimens from the coital and non-coital vagina, and from the rectum and buccal cavity, and pre-ejaculate lubricating fluid were also assayed for both enzymes. Prostatic acid phosphatase was determined with use of two substrates: thymolphthalein monophosphate and alpha-naphthyl phosphate (tartrate-inhibitable fraction). Glutamyltransferase was assayed with gamma-glutamyl-p-nitroanilide as substrate. All non-coital specimens were negative for glutamyltransferase activity; the activity of acid phosphatase varied with type of substrate and type of specimen. The equation y = a + (b/x) describes the decline in activity (y) of either acid phosphatase or glutamyltransferase in the vagina of healthy women post-coitally with time (x).

Acid Phosphatase↗
PubMed1986

Light microscopical localization of enzymes by means of cerium-based methods. I.V. Optimization procedures for acid phosphatase.

The earlier described cerium based histochemical reaction for acid phosphatase [Ce-Pb-reaction, Zimmermann and Halbhuber (1985)] was optimized. The target tissues (kidney, intestine) were fixed by perfusion with glutaraldehyde in cacodylate or piperazine buffer in anesthetized animals. Postfixation of prefixed sections is not advantageous because of the detectable repressing of the enzyme activity. Moreover, the employment of unfixed cryostat sections, which were postfixed, was always connected with a complete abolition of the acid phosphatase activity. The optimal concentration of the primary capture cerium III chloride in the incubation medium is about 1 mmol. Lower concentrations lead to an incomplete histochemical detection of phosphatase activity in lysosomes. The treatment of cryostat sections of perfusion fixed tissue with borohydride (diminution of aldehyde induced cross links) or with dimethylsulfoxide (extraction of lysosomal materials or the well known vehicle property) brought about an improvement of the penetration capacity for cerium-III-cations into the target structures. After conversion of the cerium phosphate (primary specific reaction product) into cerium perhydroxide, oxalate or fluoride, the Ce-Pb-reaction was negative. Therefore, these blocking reactions represent specific inhibition controls, which indicates the formation and presence of cerium phosphate. On the basis of these reactions it is possible to check the specificity of the histochemical Ce-Pb-reaction for phosphatase activity in sections.

Acid Phosphatase↗
PubMed1989

Visualization of acid phosphatase activity on nitrocellulose filters following electroblotting of polyacrylamide gels.

A method for visualizing acid phosphatase isoenzymes by activity staining on nitrocellulose filters after electroblotting of proteins fractionated on nondenaturing polyacrylamide gels is described. Reproducible results were obtained when 25 mM Tris-192 mM glycine was used as the transfer buffer instead of 0.7% acetic acid, 50 mM sodium acetate, pH 4, or 0.14 M acetic acid--0.35 M beta-alanine, pH 4.3. Dot-blot analysis of banana fruit extracts on nitrocellulose filters revealed that a minimum of 5 x 10(-3) units (nmol p-nitrophenyl phosphate hydrolyzed g-1.h-1) of acid phosphatase activity can be detected. This method can be suitable for screening a large number of biological samples for monitoring acid phosphatase activity.

Acid Phosphatase↗
PubMed1979

Chemoarchitectonics in a reptilian cerebral hemisphere--acid phosphatase and 5'-nucleotidase.

Variations on the distribution of acid phosphatase and 5'-nucleotidase were observed among the cerebral nuclei of the Uromastix hardwickii. Most of the nuclei revealed more intensely positive reaction for 5'-nucleotidase than the acid phosphatase. However, an identical enzymatic pattern, demonstrating intense activity for the two enzymes, was observed in the cortical centers excepting the primordial hippocampus. The possible causes of the intensity and the functions of the enzymes were established in relation to the nuclei and fiber bundles.

Acid Phosphatase↗
PubMed1976

Clinical significance of serum acid phosphatase levels in advanced prostatic carcinoma.

This cooperative study was sponsored by the National Prostatic Cancer Project to determine the usefulness of serum acid phosphatase levels as a predictive indicator with regard to performance status, sites of metastases, response to treatment, and survival in patients with advanced prostatic carcinoma. The results indicate that survival was significantly shorter for those patients who had elevation of thier on-study (pretreatment) total serum acid phosphatase ler cent reduction of primary tumor mass, relief of pain, and acid phosphatase activity. No correlation could be demonstrated between serum acid phosphatase and performance status, site of metastases, and other criteria of response to therapy. It is concluded that this test as currently determined spectrophotometrically at this stage of disease and if employed alone is not sufficient to allow for total evaluation of the response of therapy. It is, however, helpful when used in correlation with the previously mentioned positive factors.

Acid Phosphatase↗
PubMed1996

Molecular characterization of the lysosomal acid phosphatase from Drosophila melanogaster.

In Drosophila, unlike humans, the lysosomal acid phosphatase (Acph-1) is a non-essential enzyme. It is also one of the most rapidly evolving gene-enzyme systems in the genus. In order to determine which parts of the enzyme are conserved and which parts are apparently under little functional constraint, we cloned the gene from Drosophila melanogaster via a chromosomal walk. Fragments from the gene were used to recover an apparently full-length cDNA. The cDNA was sub-cloned into a Drosophila transformation vector where it was under the control of the 5' promoter sequence of the hsp-70 gene. Three independent transformants were obtained; in each, Acph-1 expression from the cDNA was constitutive and not dependent on heat shock, as determined by densitometric analyses of the allozymic forms of the enzyme. The pattern of expression indicates the hsp-70 and endogenous Acph-1 promoters act together in some, but not all, tissues. The sequence of the cDNA was determined using deletions made with exonuclease III, and primers deduced from the cDNA sequence were used to sequence the genomic clone. Five introns were found, and putative 5' upstream regulatory sequences were identified. Amino acid sequence comparisons have revealed several highly conserved motifs between Drosophila Acph-1 and vertebrate lysosomal and prostatic acid phosphatases.

Acid Phosphatase↗
PubMed1984

Neutrophil acid phosphatase activity in patients with gastric or rectum carcinoma during surgical treatment.

In 22 patients with alimentary tract carcinoma granulocyte acid phosphatase activity was determined using the histochemical method of Suzuki. Enzyme activity was determined in peripheral blood 3 times, viz. before surgical intervention, in blood from a vessel draining the tumour before its excision, and in peripheral blood 2-3 weeks after excision of the tumour. In parallel tests, enzyme activity was established in peripheral blood of 22 healthy individuals. The results showed that acid phosphatase activity of granulocytes is lower than in the controls, especially in granulocytes collected from the vessel draining the tumour. The lower acid phosphatase activity in granulocytes from patients with carcinoma was mainly due to the lower percentage of positive cells. After removal of the tumour acid phosphatase activity of the granulocytes increased in the majority of cases. It is assumed that an enhanced exocytosis of lysosomal enzymes in the course of tumour disease was responsible for the decrease of activity in the granulocytes.

Acid Phosphatase↗
PubMed1995

Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases.

The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)-Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)-Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two beta alpha beta alpha beta motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed.

Acid Phosphatase↗
PubMed1985

Repressible acid phosphatase from yeast efficiently dephosphorylates in vitro some phosphorylated proteins and peptides.

Highly purified repressible acid phosphatase from Saccharomyces cerevisiae very efficiently dephosphorylates 32P-histones and the phosphopeptides Arg-Arg-Ala-Ser-(32P)-Val-Ala and Arg-Arg-Leu-Ser (32P)-Leu-Arg previously phosphorylated by either cAMP-dependent protein kinase or protein kinase-C. The Km values (0.03-1 microM) are very favourable if compared with those calculated for free phosphoaminoacids and p-nitrophenylphosphate which are three to six orders of magnitude higher. While also the phosphopeptide Asp-Ala-Gly-Tyr(32P)-Ala-Arg3-Gly is readily dephosphorylated, other phosphopeptides and phosphoproteins including phosphorylase kinase, phosvitin and casein phosphorylated by both casein kinase 1 and 2 are not appreciably affected by acid phosphatase. It is suggested that yeast repressible acid phosphatase may act in vivo as a phosphoprotein phosphatase.

Acid Phosphatase↗
PubMed2005

An acid phosphatase from Manihot glaziovii as an alternative to alkaline Phosphatase for molecular cloning experiments.

An acid phosphatase, free of deoxyribonuclease activity, was isolated from Manihot glaziovii leaves. It had a Mr of 78 kDa and was optimally active at pH 4.3 and 52 degrees C. It was inactivated at 65 degrees C over 15 min. It had a broad substrate specificity with strongest activity towards p-nitrophenyl phosphate. The enzyme dephosphorylated linearized pUC18 DNA and preventing self-ligation under the same conditions used for calf intestine alkaline phosphatase.

Acid Phosphatase↗
PubMed1991

Measurement of prostate-specific antigen and prostatic acid phosphatase concentrations in serum before and 1-42 days after transurethral resection of the prostate and orchidectomy.

Preoperative intra-individual variation for determinations of prostate-specific antigen and prostatic acid phosphatase concentrations, 15-30% in 92 patients with benign prostatic hyperplasia, limits the diagnostic usefulness of both tumor markers. In benign prostatic hyperplasia (214 patients), concentrations of these tumor markers increased in the initial postoperative period. Prostatic acid phosphatase concentration then decreased by the third postoperative day. Prostate-specific antigen concentration remained above normal in the first postoperative week but had decreased by 42 days. In prostatic carcinoma (46 patients), the concentrations of these tumor markers did not increase postoperatively. During the first week, the concentrations of prostatic acid phosphatase began to fall, but prostate-specific antigen showed a decrease only at 42 days. After orchidectomy (11 patients), the concentrations of both markers had decreased by five days. Concentrations of prostate-specific antigen but not of prostatic acid phosphatase were significantly increased in patients with metastases at 42 days postoperatively. When the concentration of tumor marker did decrease, the magnitude of change was greater for prostatic acid phosphatase than for prostate-specific antigen. These changes were accentuated after an orchidectomy.

Acid Phosphatase↗
PubMed1980

Cytochemical investigation on acid phosphatase activity in cerebral arteries in spontaneously hypertensive rats.

Acid phosphatase activity in the cerebral arterial system in spontaneously hypertensive rats (SHR) was cytochemically investigated. In the endothelial and medial smooth muscle cells, endoplasmic reticulums and Golgi complex revealed an intense acid phosphatase activity and primary lysosomes containing the high enzyme activity were found to be augmented in number. The enzyme activity was demonstrated in the vacuolated secondary lysosomes and in the intercellular spaces of the arterial walls. Lytic changes of the arterial mural cells and vessel matrix due to lysosomal enzymes were also evident. Causes of the lysosomal enzyme induction and roles of the enzyme in the developmental mechanism of hypertensive cerebrovascular changes in the SHR brain are discussed.

Acid Phosphatase↗
PubMed1993

Assignment of the mouse tartrate-resistant acid phosphatase gene (Acp5) to chromosome 9.

Tartrate-resistant acid phosphatase is a marker enzyme for osteoclasts, the multinucleated cell responsible for bone resorption. Interspecific somatic whole cell hybrids and karyotypically simple microcell hybrids were used to map the gene encoding tartrate-resistant acid phosphatase (Acp5) to mouse Chromosome 9. Acp5 is therefore a member of a syntenic family of genes that map to human chromosome 19p13.1-p13.3 and mouse Chromosome 9.

Acid Phosphatase↗
PubMed1984

Acid phosphatase activity in the chick ovary during embryonic development.

Acid phosphatase activity was studied in the left and right ovaries of the chick during embryonic development. The cytochemical study indicated that local enzymatic activity is localized mainly in germ and somatic cells. From the results obtained in the study on the specific activity of this acid hydrolase, it can be inferred that the higher concentration of this enzyme in the right ovary would be determined by a decrease of total proteins in the total homogenate and in the cellular fractions of this organ. Besides, a decrease in the enzymatic activity of this ovary is not observed, but it occurs in the left ovary. This finding would indicate a lack of enzymatic segregation that could be related to the phenomenon of ovarian atrophy. Finally, the electrophoretic study indicated that it would apparently exist only one molecular form of the enzyme. Our results support the hypothesis that acid phosphatase would be involved in the atrophic processes of the right ovary during embryonary differentiation.

Acid Phosphatase↗
PubMed1987

Clinical significance of tartrate-sensitive and tartrate-resistant acid phosphatase indicated from the study of their biosynthetic mechanism.

The tartrate-sensitive prostatic acid phosphatase, bands 2 and 4, are found in the soluble cytosol, and absent in the polysome of the prostate, while the tartrate-resistant acid phosphatase band 5 is present in the polysome and the soluble cytosol of hairy cells. The mRNA isolated from the prostate catalyzes the incorporation of 3T leucine into a protein different from that of bands 2 and 4. On the other hand, the mRNA isolated from the hairy cells catalyzes the incorporation of 3T leucine into band 5. The different biosynthetic mechanism of these two types of acid phosphatases are discussed in light of their different clinical significance.

Acid Phosphatase↗
PubMed1997

Acid phosphatase activity in Malpighian tubules of Triatoma infestans Klug.

Acid phosphatase activity was detected in the Malpighian tubules of the blood-sucking hemipteran, Triatoma infestans. The enzyme activity was especially prominent in the cytoplasmic globules which were assumed to be laminated 'concretions', which occur in the distal cells of the organ. It was also verified in the nuclei and in some cytoplasmic granules (lysosomes) of the proximal cells. The data indicated that lysosomes were involved with the nature or origin of the laminated concretions, but it is still questionable whether acid phosphatase activity exists in the nuclei.

Acid Phosphatase↗
PubMed1987

Stimulatory effect of mevinolin on rat liver phosphatidic acid phosphatase.

The activity of the soluble form of phosphatidic acid phosphatase in rat liver was stimulated about 2.5-fold by inclusion of mevinolin, a competitive hydroxymethylglutaryl-CoA reductase inhibitor, in the diet (0.1%). The stimulatory effect of mevinolin was present also after dietary addition of cholestyramine (5%) or intraperitoneal administration of ethanol. Addition of cholesterol (2%) to the diet totally abolished the stimulation by mevinolin on phosphatidic acid phosphatase. The results support a correlation between the synthesis of the rate-limiting enzyme in cholesterol biosynthesis and the activity of the apparent rate-limiting enzyme in triacylglycerol biosynthesis.

Acid Phosphatase↗