Results 261 to 270 of about 67,703 (305)

Viral adenosine triphosphatase [PDF]

open access: possibleExperientia, 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
Some of the next articles are maybe not open access.

Related searches:

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   +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

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
openaire   +3 more sources

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
openaire   +3 more sources

Home - About - Disclaimer - Privacy