scholarly journals The hydrolysis of phenyl phosphate by mouse-liver acid phosphatase

1961 ◽  
Vol 80 (1) ◽  
pp. 154-161 ◽  
Author(s):  
K MACDONALD
Keyword(s):  
Acid Phosphatase ◽  
Mouse Liver ◽  
Phenyl Phosphate ◽  
Hydrolysis Of

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.

Further Observations upon the Oxyntic Cells with Special Reference to Acid Phosphatase

1952 ◽  
Vol s3-93 (23) ◽  
pp. 259-268
Author(s):  
GORDON MENZIES
Keyword(s):  
Acid Phosphatase ◽  
Special Reference ◽  
Single Injection ◽  
Central Area ◽  
Basal Part ◽  
Prolonged Starvation ◽  
Apparent Change ◽  
Multiple Doses ◽  
Hydrolysis Of ◽  
In Cells

1. In continuation of work already reported (Menzies, 1949) further data are presented on the structure and cyto-chemistry of the granules in the oxyntic cells of the rat's stomach. 2. After multiple doses of pilocarpine or histamine, and after feeding, the phospholipine (as shown by acid haematein) is shed from some or all of the granules. The lipine first leaves the granules in cells situated in the basal part of the tubules, and finally those in the neck of the tubules, but a non-lipine lipoid remains in all the granules (as shown by sudan black). 3. The granules enlarge after prolonged starvation as they do after a single injection of pilocarpine; but after extraction of lipoids by hot pyridine and subsequent straining with iron haematoxylin, enlargement (i.e. of the non-lipoid moiety) is shown only after prolonged starvation. 4. A light, uncoloured central area is found in some of the largest granules after feeding and colouring with acid haematein. 5. An acid phosphatase appears in the oxyntic cells whose granules are about to lose their lipine component, and it disappears when they have done so. It is suggested that the acid phosphatase may cause hydrolysis of the phospholipine. 6. Only after prolonged starvation is there any apparent change in granule numbers, when they are decreased.

Recent findings in oogenesis of Drosophila melanogaster

Development ◽  
1977 ◽  
Vol 39 (1) ◽  
pp. 45-57
Author(s):  
F. Giorgi ◽  
J. Jacob
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Ovarian Development ◽  
Superficial Layer ◽  
Blood Proteins ◽  
Selective Hydrolysis ◽  
Internal Lining ◽  
Hydrolysis Of ◽  
Zinc Iodide ◽  
Yolk Platelet

The role played by the vitellogenic oocytes of Drosophila melanogaster in relation to the elaboration of material taken from the haemolymph is examined by ultrastructural cytochemistry. As revealed by the Gomori procedure, acid phosphatase occurs widely over the forming yolk platelets of the cortical and central ooplasm. A number of Golgi apparatuses in thecortical ooplasm are also positively stained with lead precipitates. With the proceeding of the ovarian development it becomes progressively more difficult to demonstrate cytochemically the enzyme over the yolk platelets. In stage 9–10 chambers the acid phosphatase is restricted to the so-called associated body, while the rest of the yolk platelet appears devoid of lead deposits. By using a osmium zinc iodide (OZ1) complex as a preferential staining method for the Golgi apparatus, it has been shown that, apart from the apparatus itself, a number of OZI deposits occur over the superficial layer of the forming yolk platelets. When mature yolk platelets are formed at later stages, the OZI deposits in the yolk platelets come to be restricted to the cap-like region of the superficial layer which contains the associated body. In vitellogenic oocytes, both the internal lining of the limiting membrane of the forming yolk platelets and the associated body of the mature yolk platelets react positively, to cytochemical methods to demonstrate carbohydrates. The present findings are interpreted as indicating the involvement of lysosomal enzymes in the process of maturation of the yolk material. The suggestion is also made that such an involvement is required to accomplish a selective hydrolysis of those blood proteins which have been taken in by vitellogenic oocytes along with yolk precursors.

Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.

1977 ◽  
Vol 23 (1) ◽  
pp. 89-94 ◽  
Author(s):  
K W Lam ◽  
L T Yam
Keyword(s):  
Acid Phosphatase ◽  
Biochemical Characterization ◽  
Normal Animal ◽  
Tartrate Resistant Acid Phosphatase ◽  
Animal Tissues ◽  
Human Spleen ◽  
Optimal Activity ◽  
Catalytic Function ◽  
Hydrolysis Of

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.

Enhancing Effect of Surfactant and Protein on Hydrolysis of Thymolphthalein Monophosphate by Purified Prostatic Acid Phosphatase

1975 ◽  
Vol 21 (12) ◽  
pp. 1761-1765 ◽  
Author(s):  
Andras G Foti ◽  
Harvey Herschman ◽  
J Fenimore Cooper ◽  
Hedi imFeld
Keyword(s):  
Acid Phosphatase ◽  
Serum Proteins ◽  
Gradient Centrifugation ◽  
Gel Filtration ◽  
Prostatic Acid Phosphatase ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation ◽  
Brij 35 ◽  
Hydrolysis Of ◽  
Protein Bovine Serum Albumin

Abstract Purified prostatic acid phosphatase catalyzes the hydrolysis of thymolphthalein monophosphate 10-fold faster if an optimal concentration of Brij 35 (a wetting agent) or protein (bovine serum albumin or human serum proteins) is present. Results of gel filtration, dialysis, and sucrose density-gradient centrifugation analysis suggest that the substrate must combine with detergent or protein before the enzyme can catalyze its hydrolysis.

scholarly journals LOCALIZATION OF PEROXIDASE ACTIVITY IN MICROBODIES OF FETAL MOUSE LIVER

1969 ◽  
Vol 17 (7) ◽  
pp. 454-466 ◽  
Author(s):  
EDWARD ESSNER
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Peroxidase Activity ◽  
Mouse Liver ◽  
Fetal Liver ◽  
Light And Electron Microscopy ◽  
Small Population ◽  
Fetal Mouse ◽  
Fetal Mouse Liver

The peroxidase activity of microbodies in fetal mouse liver was studied by light and electron microscopy. Two types of microbodies were present; a small population of bodies that lacked a nucleoid, predominant on the 16th day of gestation, and a larger population of nucleoid-bearing microbodies, predominant on the 19th day, in association with the rough endoplasmic reticulum from which they probably originate. Both types of bodies were visualized when incubated for peroxidase activity but were negative (19th day) for acid phosphatase activity. The findings suggest that the anucleoid- and nucleoid-bearing organelles together constitute the microbody population of the fetal liver.

Reactions of acyl phosphates. Base hydrolysis of [Co(NH3)5OPO3COCH3]+ and the metal hydroxide promoted hydrolysis of acetyl phenyl phosphate

1981 ◽  
Vol 34 (8) ◽  
pp. 1769 ◽  
Author(s):  
DA Buckingham ◽  
CR Clark
Keyword(s):  
Hydroxo Complex ◽  
Metal Hydroxide ◽  
Base Hydrolysis ◽  
Acetyl Phosphate ◽  
Carbonyl Carbon ◽  
Phenyl Phosphate ◽  
Hydrolysis Of ◽  
Oxygen Bond

Tracer 18O studies have established that base hydrolysis of coordinated acetyl phosphate in [(NH3)5Co-OPO3COCH3]+ (kOH 0.53 mol-1 dm3 s-1, 25°C, I 1.0 NaClO4) proceeds with exclusive carbon-oxygen bond fission. The hydrolysis of acetyl phenyl phosphate monoanion is significantly catalysed by the exchange-inert hydroxo complex [(NH3)5Co-OH]2+ (kMOH 2.9 × 10-2 mol-1 dm3 s-1, 25°) which operates through a nucleophilic pathway involving attack at carbonyl carbon.

Polyphosphate body and acid phosphatase localization in Nostoc sp.

1984 ◽  
Vol 30 (1) ◽  
pp. 8-15 ◽  
Author(s):  
John D. DuBois ◽  
Keith R. Roberts ◽  
Lawrence A. Kapustka
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Energy Stress ◽  
Nitrophenyl Phosphate ◽  
Carbon Compounds ◽  
Electron And Light Microscopy ◽  
Polyphosphate Bodies ◽  
Hydrolysis Of

Polyphosphate bodies and acid phosphatase activity were characterized in Nostoc sp. to determine if the hydrolysis of polyphosphate bodies occurs during dark (energy stress) periods. Electron and light microscopy were used to locate polyphosphate bodies. Acid phosphatase activity was measured using p-nitrophenyl phosphate as the substrate to determine net changes in the level of the enzyme activity. To induce energy stress, Nostoc sp. cells were kept in the dark for 72 h to deplete stored carbon compounds. Cells incubated in the light for 72 h (controls) showed acid phosphatase activity localized around the perimeter of polyphosphate bodies. When cells were incubated in the dark, acid phosphatase activity occurred throughout the polyphosphate body matrix. However, complete hydrolysis of the polyphosphate body did not occur and the rate of acid phosphatase activity was not affected.

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