scholarly journals ISOZYMES OF ACID PHOSPHATASE IN NORMAL AND CALMETTE-GUÉRIN BACILLUS-INDUCED RABBIT ALVEOLAR MACROPHAGES

1968 ◽  
Vol 128 (5) ◽  
pp. 1031-1048 ◽  
Author(s):  
S. G. Axline
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alveolar Macrophages ◽  
Acid Phosphatase Activity ◽  
Enzyme Inhibitors ◽  
Freezing And Thawing ◽  
Ph Optimum ◽  
Lysosomal Fraction ◽  
Repeated Freezing ◽  
Major Acid

The acid phosphatase activity of normal alveolar and BCG-induced alveolar macrophages has been examined. Five electrophoretically distinct forms of acid phosphatase have been identified in both normal and BCG-induced macrophages. The acid phosphatases can be divided into two major categories. One category, containing four distinct forms, is readily solubilized after repeated freezing and thawing or mechanical disruption The second category, containing one form, is firmly bound to the lysosomal membrane and can be solubilized by treatment of the lysosomal fraction with Triton X-100. The Triton-extractable acid phosphatase and the predominant aqueous soluble acid phosphatase have been shown to differ in the degree of membrane binding, in solubility, in net charge, and in molecular weight. The two pre-dominant phosphatases possess identical pH optimum and do not differ in response to enzyme inhibitors. BCG stimulation has been shown to result in a nearly twofold increase in acid phosphatase activity. A nearly proportionate increase in the major acid phosphatase forms has been observed.

Acid Phosphatase Activity in Vegetative Cells and Spores of Clostridium botulinum Type E

1971 ◽  
Vol 28 (11) ◽  
pp. 1817-1820 ◽  
Author(s):  
G. A. Strasdine ◽  
Joanne M. Melville
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Clostridium Botulinum ◽  
Specific Activity ◽  
Growth Media ◽  
Ph Optimum ◽  
Vegetative Cells ◽  
Botulinum Type ◽  
Clostridium Botulinum Type E

Acid phosphatase activity with a pH optimum of 5 was demonstrated in vegetative cells, spores, and germinated spores of Clostridium botulinum type E (Minnesota). The enzyme was present in the cells during all stages of growth and was insensitive to the orthophosphate concentration of the growth media. Specific activity of the enzyme increased during growth coincident with a loss in inorganic phosphate from the acid-soluble cell fraction. Magnesium or manganese was required for maximum enzyme activity. Acid phosphatase in crude spore extracts was more heat-stable than in extracts obtained from vegetative cells.

Acid Phosphatase Activities in Developing Seeds of Pisum sativum L

1977 ◽  
Vol 4 (6) ◽  
pp. 843 ◽  
Author(s):  
DR Murray ◽  
MD Collier
Keyword(s):  
Acid Phosphatase ◽  
Pisum Sativum ◽  
Phosphatase Activity ◽  
Cell Expansion ◽  
Acid Phosphatase Activity ◽  
Minor Components ◽  
Ph Optimum ◽  
Pisum Sativum L ◽  
Almost All ◽  
Pea Seed

The seedcoats contain almost all of the acid phosphatase activity (EC 3.1.3.2) in the pea seed in the earliest stages of expansion. The seedcoat activity is maximal by the end of the period of rapid cell expansion and declines as the embryo matures. The developing cotyledons show a later rise in acid phosphatase activity to a maximum shortly before dehydration. The activity in the embryonic axis shows a marked increase only during dehydration. The acid phosphatase activity in the seedcoats results almost entirely from an isoenzyme with high electrophoretic mobility in 5.5% polyacrylamide gels (RF 0.97). This isoenzyme has not been detected in other tissues from the plant. The phosphatase activity in the cotyledons is accounted for by one major isoenzyme at RF 0.75 and by four minor components. The partially purified enzyme from the seedcoats shows a broad pH optimum from pH 5.0 to pH 6.0. In contrast, the preparation from the cotyledons has an optimum close to pH 5.6 and is slightly more sensitive to inhibition by 0.2 mM PI.

scholarly journals New form of acid phosphatase during lysosome biogenesis

1981 ◽  
Vol 198 (1) ◽  
pp. 9-15 ◽  
Author(s):  
G R Rao ◽  
H N Aithal ◽  
F G Toback ◽  
G S Getz
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Lysosomal Enzyme ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Deficient Diet ◽  
Lysosomal Fraction ◽  
K Depletion

Lysosome formation was induced in cells of the renal medulla by feeding rats on a K+-deficient diet. The role of the endoplasmic reticulum in the production of acid phosphatase, a typical lysosomal enzyme, was examined. Lysosomal and microsomal fractions were prepared for study by differential centrifugation of homogenates of renal papilla and inner stripe of red medulla. Acid phosphatase activity in the microsomal fraction was distinguished from the activity in the lysosomal fraction in normal tissue by differences in pH optima, tartrate inhibition, distribution of multiple forms after polyacrylamide-gel electrophoresis and detergent-sensitivity. During progressive K+ depletion, acid phosphatase activity in both microsomal and lysosomal fractions of the tissue increased 3-fold. In the lysosomes, K+ depletion was associated with the appearance of a new band of acid phosphatase. The neuraminidase-sensitivity of this band on polyacrylamide-gel electrophoresis indicated that the enzyme protein had been modified by the addition of sialic acid residues. K+ depletion also altered the lysosomal enzyme so that thiol compounds were able to stimulate its activity.

scholarly journals Quantitative histochemical study of acid phosphatase activity in rat liver using a semipermeable membrane technique.

1987 ◽  
Vol 35 (2) ◽  
pp. 175-180 ◽  
Author(s):  
W M Frederiks ◽  
F Marx ◽  
G N Jonges ◽  
C J Van Noorden
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity ◽  
Enzyme Inhibitors ◽  
Semipermeable Membrane ◽  
Coupling Technique ◽  
Lysosomal Acid ◽  
Membrane Technique ◽  
Post Coupling

Acid phosphatase activity has been demonstrated in rat liver with the semipermeable membrane technique using naphthol AS-BI phosphate as substrate and hexazotized pararosaniline (HPRA) as simultaneous coupling agent. With this method the final reaction product (FRP) appeared in rat liver as intensely colored red granules in liver parenchymal cells and in Küpffer cells. The absorbance spectrum of the FRP peaks between 510 and 550 nm. A nonspecific reaction product, as has been found in skeletal muscle, did not occur in rat liver. A substrate concentration of 5 mM and a HPRA concentration of 10 mM result in optimum localization and activity. We concluded from the results with different enzyme inhibitors that lysosomal acid phosphatase was demonstrated. The mean absorbance of the FRP increased linearly with incubation time (15-60 min). Furthermore, we found a linear increase of the FRP with increasing section thickness (4-10 micron). When the simultaneous coupling method was replaced by a post-coupling technique, the colored reaction product was diffusely located throughout the cytoplasm. In conclusion, the simultaneous coupling technique in combination with the semipermeable membrane method is a valuable tool for detecting and quantifying lysosomal acid phosphatase activity in rat liver. We demonstrated that acid phosphatase activity is 1.2 times higher periportally than pericentrally in rat liver, and that 24 hr fasting before the experiments did not change the acid phosphatase activity.

scholarly journals Ultrastructural study of GERL in beige mouse alveolar macrophages.

1977 ◽  
Vol 75 (2) ◽  
pp. 381-387 ◽  
Author(s):  
E Essner ◽  
H Haimes
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alveolar Macrophages ◽  
Ultrastructural Study ◽  
Acid Phosphatase Activity ◽  
Colloidal Silver ◽  
Mouse Mutant ◽  
Beige Mouse ◽  
Residual Bodies

Alveolar macrophages of the beige mouse mutant have a system of smooth-surfaced elements with the hallmarks of GERL. GERL also appears to produce residual bodies, and both organelles show cytochemically demonstrable acid phosphatase activity. When cells are exposed to colloidal silver, the tracer is endocytosed via pinocytic vacuoles to GERL.

scholarly journals Legionella pneumophila Major Acid Phosphatase and Its Role in Intracellular Infection

2001 ◽  
Vol 69 (1) ◽  
pp. 177-185 ◽  
Author(s):  
Virginia Aragon ◽  
Sherry Kurtz ◽  
Nicholas P. Cianciotto
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Legionella Pneumophila ◽  
Acid Phosphatase Activity ◽  
Intracellular Infection ◽  
Type Iv ◽  
Pilus Biogenesis ◽  
Prepilin Peptidase ◽  
Major Acid ◽  
Transposon Insertions

ABSTRACT Legionella pneumophila is an intracellular pathogen of protozoa and alveolar macrophages. This bacterium contains a gene (pilD) that is involved in both type IV pilus biogenesis and type II protein secretion. We previously demonstrated that the PilD prepilin peptidase is crucial for intracellular infection by L. pneumophila and that the secreted pilD-dependent proteins include a metalloprotease, an acid phosphatase, an esterase/lipase, a phospholipase A, and a p-nitrophenyl phosphorylcholine hydrolase. Since mutants lacking type IV pili, the protease, or the phosphorylcholine hydrolase are not defective for intracellular infection, we sought to determine the significance of the secreted acid phosphatase activity. Three mutants defective in acid phosphatase activity were isolated from a population of mini-Tn10-mutagenized L. pneumophila. Supernatants as well as cell lysates from these mutants contained minimal acid phosphatase activity while possessing normal levels of other pilD-dependent exoproteins. Genetic studies indicated that the gene affected by the transposon insertions encoded a novel bacterial histidine acid phosphatase, which we designated Map for major acid phosphatase. Subsequent inhibitor studies indicated that Map, like its eukaryotic homologs, is a tartrate-sensitive acid phosphatase. Themap mutants grew within macrophage-like U937 cells andHartmannella amoebae to the same degree as did wild-type legionellae, indicating that this acid phosphatase is not essential forL. pneumophila intracellular infection. However, in the course of characterizing our new mutants, we gained evidence for a second pilD-dependent acid phosphatase activity that, unlike Map, is tartrate resistant.

scholarly journals Heterogeneity of liver acid phosphatases in developing chick embryo

1969 ◽  
Vol 115 (2) ◽  
pp. 191-197 ◽  
Author(s):  
K.-M. Wang
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Soluble Fraction ◽  
The Other ◽  
Acid Phosphatases ◽  
Peak Activity ◽  
Ph Optimum ◽  
Triton X ◽  
Soluble Fractions

1. The development, localization and heterogeneity of acid phosphatase and a Zn2+-activated acid phosphatase in cellular fractions of developing chick liver were studied. 2. Acid phosphatase is distributed abundantly in the particulate and soluble fractions. The soluble fraction is rich in Zn2+-activated acid phosphatase, which attains its peak activity at about 15 days of incubation. 3. The particulate acid phosphatase activity is inhibited by fluoride but not by sodium l(+)-tartrate or cysteine. On the other hand, the soluble Zn2+-activated acid phosphatase activity is inhibited by sodium l(+)-tartrate and cysteine but not by fluoride. 4. The pH optimum of these two enzymes is similar at about 5·6. 5. The soluble Zn2+-activated acid phosphatase activity appears to be thermally stabilized by the treatment with Triton X-100 or bovine serum albumin.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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