Results 141 to 150 of about 38,432 (164)
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Adenosine triphosphatase in the phloem of Cucurbita

Planta, 1973
The distribution of adenosine triphosphatase (ATPase) activity in the phloem of petioles and minor veins of Cucurbita maxima has been studied using a lead phosphate precipitation procedure. ATPase activity was localized in sieve elements, companion cells and parenchyma cells.
Jamison Gilder, James Cronshaw
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Thiamine triphosphatase in the nervous system

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1972
Abstract Thiamine triphosphate is hydrolyzed by a specific triphosphatase in subcellular fractions of rat brain. This enzyme differs from nucleoside triphosphatases in (1) its subcellular distribution pattern; (2) its susceptibility to inhibition by Ca 2+ ; (3) its activation by sodium deoxycholate; (4) its failure to be affected by known inhibitors ...
Peter E. Braun, Robert L. Barchi
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The adenosine triphosphatase activity of the meromyosins

Biochimica et Biophysica Acta (BBA) - Enzymology, 1967
Abstract 1. 1.|Mg 2+ does not activate the ATPase (ATP phosphohydrolase, EC 3.6.1.3) of actin-heavy meromyosin complex (acto-HMM) at low ionic strength. 2. 2.|The interaction inhibitor heparin, which dissociates actomyosin and inhibits its ATPase activity, also inhibits the ATPase of acto-HMM. 3.
Andras Muhlrad, S. Bosko, N.A. Biró
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Ribonucleoside triphosphatase in rabbit reticulocytes

Archives of Biochemistry and Biophysics, 1966
Ribonucleoside triphosphatase in rabbit reticulocytes, discussing distribution in extracts, behavior in purification of amino acid and ...
I.D. Raacke, S. Matsushita, J. Fiala
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Diseases of Renal Adenosine Triphosphatase

The American Journal of the Medical Sciences, 1995
Most renal transport is a primary or secondary result of the action of one of three membrane bound ion translocating ATPase pumps. The proximal tubule mechanisms for the reabsorption of salt, volume, organic compounds, phosphate, and most bicarbonate reabsorption depend upon the generation and maintenance of a low intracellular sodium concentration by ...
Neil A. Kurtzman   +2 more
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Deoxyuridine triphosphatase in human hepatoma

International Journal of Biochemistry, 1994
1. Deoxyuridine triphosphatase (dUTPase) in human hepatoma was investigated. The apparent activity in a gram weight tissue was about 6 times that of the activity in rat livers after partial hepatectomy. 2. Most catalytic properties of the hepatoma dUTPase were similar to the enzymes from other sources. 3.
Koyama Iwao   +3 more
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Pharmacogenetic Significance of Inosine Triphosphatase

Pharmacogenomics, 2007
Inosine triphosphatase (ITPase) is the enzyme that catalyzes the conversion of inosine triphosphate (ITP) and deoxy-inosine triphosphate (dITP) to inosine monophosphate and deoxy-inosine monophosphate, respectively, thereby maintaining low intracellular concentrations of ITP and dITP.
Martijn Lindhout   +2 more
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Adenosine triphosphatase distribution in mammary tissue [PDF]

open access: possibleThe Histochemical Journal, 1978
Lactating mammary tissue from farm animals and small mammals was perfusion-fixed, prior to histochemical procedures, in an effort to localize the ouabain-sensitive Na+/K+-stimulated ATPase enzyme with the use of specific inhibitors. Histochemical evidence suggests that the Na+/K+-stimulated ATPase is located predominantly on the cytoplasmic side of the
F. B. P. Wooding, M. P. Johnson
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Structure of the Vacuolar Adenosine Triphosphatases

Cell Biochemistry and Biophysics, 2001
Vacuolar adenosine triphosphatases (V-ATPases) represent an important class of proton pumps found in endomembrane systems of eucaryotic cells, where they are involved in pH regulation. Progress has been made in the structure determination of this large, membrane-bound multisubunit enzyme complex.
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Mitochondrial adenosine triphosphatase

Journal of Bioenergetics, 1975
Subuni ts . . . . . . . . . . . . . . . . . . . . . . 250 Number . . . . . . . . . . . . . . . . . . . . . 250 Molecular weight and s to ich iomet ry . . . . . . . . . . . . . 251 Isola t ion and amino acid compos i t ion . . . . . . . . . . . . 252 Impuri t ies or products o f proteolysis . . . . . . . . . . . . . 255 Biogenesis . . . . . . . . . . . .
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