Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.25 (triphosphatase)
 1,529 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cytologic features of a highly malignant sarcomatous tumor in a 37-year-old male, arising from interdigitating cells and localized in the mediastinum, lymph nodes and skin, are described. Cytologically this sarcoma was characterized by large cells with ill-defined, faintly basophilic cytoplasm, monocytoid or multilobulated nuclei and a reticular chromatin structure; very prominent nucleoli were seen in some of the cells. Some of the tumor cells were spindle shaped. The ultrastructurally characteristic invaginations of the cell membrane were not obvious in the cytologic smear, although the nuclear membrane showed deep, narrow, channel-like indentations. The specific ultrastructural, immunologic and cytochemical characteristics of the interdigitating cells were recognized in the tumor cells. Adenosine triphosphatase was present in the tumor cells in large amounts, while acid phosphatase, acid alpha-naphthyl acetate esterase and other enzymes were absent. The described tumor must be considered another tumor of the mononuclear phagocyte system; the proposed name is "interdigitating-cell sarcoma."
 ...
PMID:Sarcoma arising from interdigitating cells. Cytology and cytochemistry. 622 76

Adenosine triphosphatase (ATPase) activity of flagella isolated from ejaculated bull sperm was solubilized by 5 min exposure to 0.6 M KCl at 4 degrees C. ATPase activity in the flagellar extract was characterized with respect to enzyme, substrate, activator ion, salt, and hydrogen ion concentration. Flagellar extract required the presence of a divalent cation for activity: Mg2+, Ca2+, or Mn2+ could function as activator, but Zn2+ or Cd2+ could not. Magnesium-activated ATPase was maximal in the presence of Mg2+ and ATP in equimolar concentrations and at alkaline pH. Calcium activated ATPase was maximal over a wide range of Ca2+:ATP ratios and at pH 8.0. The presence of increasing concentrations of Na+ and/or K+ ions in the assay medium (0.5-300 mM) had no effect on the ATPase activity of flagellar extract.
 ...
PMID:Studies on the flagellar ATPase of bull spermatozoa: extraction and characterization. 622 99

Adenosine triphosphatase (ATPase) activity and acid phosphatase activity in lymphocytes from patients with carcinoma of the gastrointestinal tract were determined in order to investigate whether or not changes in these enzyme activities has any relation to the immune reactivity of carcinoma-bearing patients. In patients with a performance status of more than 60%, the mean value of the total ATPase activity in lymphocytes differed little from that in controls, but the mean value of the oligomycin-sensitive ATPase activity decreased as compared to that in the controls. On the other hand, the mean values of the activities of both free and total acid phosphatase in lymphocytes increased as compared to those in controls. The mean values of the activities of both ATPase and acid phosphatase in lymphocytes from patients whose performance status was less than 50% decreased as compared to those from controls and patients whose performance status was more than 60%. The change of the activities of both ATPase and acid phosphatase in lymphocytes has relation to that of the immunological parameters of the patients with carcinoma of the gastrointestinal tract. These results indicate that both ATPase and acid phosphatase in lymphocytes may play an important role in the immune mechanism.
 ...
PMID:Changes of enzyme activities recognized in lymphocytes from patients with carcinoma of the gastrointestinal tract. 622 54

The soluble form of mitochondrial adenosine triphosphatase was purified in an electrophoretically and immunologically pure form from sweet potato root tissue. The enzyme consisted of six kinds of subunits with different molecular weights (52,500, 51,500, 35,500, 26,000, 23,000, and 12,000), and its molecular weight was about 370,000. Adenosine triphosphatase associated with the submitochondrial particles was oligomycin-sensitive and heat-labile, whereas the soluble form of the enzyme was oligomycin-insensitive and cold-labile. The enzyme in either the membrane-bound or the soluble form showed negative cooperativity. Both experiments with polyacrylamide gel electrophoresis and immunological methods suggest that some of the subunits, probably those with molecular weights of 52,500 and 51,500, are dissociated from the enzyme protein during storage of the enzyme preparations.
 ...
PMID:Purification and characterization of the soluble form of mitochondrial adenosine triphosphatase from sweet potato. 622 90

In vitro movement of fibrils composed of actin and myosin filaments purified from skeletal muscle was observed by dark field microscopy during superprecipitation at low ionic strengths at room temperature. The movement was activated by phosphorylation of light chain (LC2) of myosin. The activity of the movement was evaluated in terms of the spreading of the area where the fibrils were moving. Adenosine triphosphatase activity of actomyosin was also enhanced by phosphorylation of LC2 and was correlated with the activity of the in vitro movement.
 ...
PMID:Phosphorylation of myosin light chain modulates the in vitro movement of fibrils composed of actin and myosin filaments from skeletal muscle. 622 49

Adenosine triphosphatase activity which is Mg2+-dependent and stimulated by submicromolar concentrations of Ca2+ (as Ca . ATP) was identified in the total particulate fraction of rat pancreatic acini. Half-maximal activity (V0.5) is obtained at 100.1 +/- 6 nM Ca . ATP with a Hill coefficient of 2.2 +/- 0.1 (mean +/- S.E.; n = 4). Maximal activity was 75 +/- 19 pmol of Pi released from ATP minute-1 microgram of membrane protein-1 (mean +/- S.E.; n = 7). High affinity Ca2+-ATPase activity was unaffected by ouabain, Na+, K+, La3+, and added calmodulin. Activity was slightly reduced by ruthenium red (0.1 mM) and by oligomycin (80 micrograms/ml) but was reduced almost 50% by the phenothiazine derivative fluphenazine in a dose-related and Ca2+-dependent manner. Hydrolysis of p-nitrophenyl phosphate was 9% of the rate of ATP hydrolysis and was independent of Ca2+ concentration. However, ADP, GTP, UTP, and ITP were hydrolyzed at 76-93% the rate that ATP was hydrolyzed with V0.5 values and Hill coefficients similar to those of Ca . ATP. We conclude that rat pancreatic acini contain an enzyme for active Ca2+ translocation: ATPase activity that is Mg2+-dependent and stimulated by submicromolar concentrations of Ca . ATP. Substrate hydrolysis appears to involve positive cooperative interactions of multiple ligand-binding sites and may be regulated in part by calmodulin.
 ...
PMID:High affinity, calcium-stimulated adenosine triphosphatase activity in the particulate fraction of rat pancreatic acini. 623 78

Cells of the intercalary ducts showed concentrations of secretory granules adjacent to the luminal plasma membrane. Evidence of thiamine-pyrophosphatase activity was seen in the Golgi apparatus and of acid-phosphatase activity in GERL-like structure, lysosomes and immature secretory granules. Adenosine-triphosphatase reaction-product was present along surfaces of myoepithelial cells and to a lesser extent along contiguous surfaces of duct cells. The findings indicate secretory activity in the intercalary duct cells.
 ...
PMID:Ultrastructural phosphatase cytochemistry of the intercalary ducts of the parotid and submandibular salivary glands of man. 628 Jun 55

Adenosine triphosphatase activity of U. urealyticum is an integral membrane-bound protein which cannot be detached from the membrane by mild treatment with EDTA in low-ionic strength media nor by ionic detergents which rapidly inactivated the enzyme. The enzyme was Mg++ dependent; Mn++ and Co++ could replace Mg++ to some extent. A slight stimulatory effect was also exerted by sodium and lithium. The enzyme showed a nucleotide triphosphatase activity, but ADP was hydrolyzed at close to 40% the rate of ATP and other nucleotide monophosphatase were hydrolyzed at a very slow rate. Oubain and oligomycin did not inhibit the adenosine triphosphatase activity, whereas DCCD, NBD-Cl and several sulfhydryl-blocking reagents strongly reduced its activity. The enzyme could not be stimulated by trypsin pretreatment. It seems that the complex enzyme is tightly linked to the lipid bilayer of the membrane and differs in many aspects from the F0-F1 (Mg++, Ca++)-ATPase of bacteria.
 ...
PMID:Adenosine triphosphatase activity of Ureaplasma urealyticum. 628 75

The development of colonic water and electrolyte transport was studied in rats. The colon of 20-day-old (young) and 40-day-old (adult) rats was perfused with either a hypotonic (200 mosmol/L) or a hypertonic (450 mosmol/L) solution. The solutions had identical electrolyte contents. Polyethylene glycol was used as a marker of water absorption. Na,K-Adenosine triphosphatase (Na,K-ATPase) activity was determined in nonperfused colonic segments in 10- to 40-day-old rats. Water absorption was always higher in young rats than in adult rats. In the young rats but not in the adult rats increased osmotic pressure of the luminal fluid resulted in a significant decrease in water absorption. The secretion of K was observed only in adult rats. Na,K-ATPase activity increased significantly from 10 to 20 and from 20 to 40 days of age. The results imply that the immature colon has higher water conductivity and low active electrolyte transport.
 ...
PMID:Colonic water and electrolyte transport in young and adult rats. 633 Mar 39

Electron microscopy cytochemistry has been used to study the cytoplasmic location of liposomes and lipid vesicles following specific antibody-dependent phagocytosis. The vesicle compositions were 94-99 mol% 'fluid' lipid (egg phosphatidylcholine or dimyristoylphosphatidylcholine at 37 degrees C or 'solid' lipid (dipalmitoylphosphatidylcholine at 37 degrees C). In some cases, 4 mol% phosphatidylserine was included in the vesicle membrane so as to vary the surface charge density. These vesicles undergo specific antibody-dependent phagocytosis by RAW264 macrophages when the lipid membranes contain 1-2 mol% dinitrophenyl lipid hapten in the presence of rabbit anti-dinitrophenyl IgG antibody. Internalized lipid vesicles can be visualized with the electron microscope when ferritin is trapped in the internal aqueous compartments prior to internalization. The lipid vesicles were demonstrated to be internal to the macrophage plasma membranes by selectively staining the plasma membranes with Ruthenium red. The cytoplasmic location of vesicles and liposomes was studied by electron microscopic staining for activities of the following enzymes: (1) acid phosphatase; (2) inorganic trimetaphosphatase; (3) adenosine triphosphatase; and (4) glucose-6-phosphatase. The first two enzymatic activities were found in association with ferritin-containing vesicles after antibody-dependent phagocytosis, showing the formation of vesicle-containing phagolysosomes. Adenosine triphosphatase and glucose-6-phosphatase were primary not associated with the vesicles, suggesting a minimal association of vesicles with plasma membrane, Golgi, endoplasmic reticulum and perinuclear cisternae. Phagosome-lysosome fusion did not appear to depend on the type of target lipid vesicle or liposome, on the 'fluidity' of the target membrane, or the presence of phosphatidylserine in the target membrane.
 ...
PMID:Cytochemical study of liposome and lipid vesicle phagocytosis. 668 37


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>