Results 261 to 270 of about 57,313 (306)

Membrane adenosine triphosphatase of Micrococcus lysodeikticus. Purification, properties of the "soluble" enzyme and properties of the membrane-bound enzyme.

, 1969
Emilio Muñoz, M.R.J. Salton, Mun Hon Ng, M. T. Schor   +3 more
openalex  

Duodenal Foveolar Adenoma: Case Presentation with Whole Exome Sequencing and Review of the Literature.

Pathobiology
Ferenczi Á, Germano S, Afonso J, Kuthi L, Lantos T, Sejben A.   +5 more
europepmc   +1 more source

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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 ...
J. Bierau, M. Lindhout, J. Bakker
semanticscholar   +4 more sources

Viral adenosine triphosphatase [PDF]

Experientia, 1978
The catalytic and immunological properties of an adenosine triphosphatase from different types of virus have been studied. The avian myeloblastosis virus has been found to be specialized in holding this enzyme in a highly active state as compared to other virus with respect to their host cell enzyme.
openaire   +2 more sources

Brain capillary guanosine triphosphatase: A distinction from adenosine triphosphatase

Experientia, 1980
Differences in kinetic properties, pH response, sensitivity to ouabain, and disc-acrylamide electrophoresis resolution, are observed when GTP and ATP are used as the substrates for triphosphohydrolases in isolated rat brain microvessels. In brain parenchyma there are no such differences.
B. B. Mršulja, T. Stojanović, B. M. Djuričić   +2 more
openaire   +3 more sources

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
openaire   +3 more sources

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
openaire   +3 more sources