Results 271 to 280 of about 57,313 (306)
Some of the next articles are maybe not open access.
The adenosine triphosphatase activity of the meromyosins
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967Abstract 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, 1966Ribonucleoside 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
Science, 1988
A cytoplasmic protein that greatly enhances the guanosine triphosphatase (GTPase) activity of N-ras protein but does not affect the activity of oncogenic ras mutants has been recently described. This protein (GAP) is shown here to be ubiquitous in higher
Hedy Adari +4 more
semanticscholar +1 more source
A cytoplasmic protein that greatly enhances the guanosine triphosphatase (GTPase) activity of N-ras protein but does not affect the activity of oncogenic ras mutants has been recently described. This protein (GAP) is shown here to be ubiquitous in higher
Hedy Adari +4 more
semanticscholar +1 more source
Diseases of Renal Adenosine Triphosphatase
The American Journal of the Medical Sciences, 1995Most 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
openaire +3 more sources
Science, 1990
The TFP1 gene of the yeast Saccharomyces cerevisiae encodes two proteins: the 69-kilodalton (kD) catalytic subunit of the vacuolar proton-translocating adenosine triphosphatase (H(+)-ATPase) and a 50-kD protein. The 69-kD subunit is encoded by the 5' and
Patricia M. Kane +8 more
semanticscholar +1 more source
The TFP1 gene of the yeast Saccharomyces cerevisiae encodes two proteins: the 69-kilodalton (kD) catalytic subunit of the vacuolar proton-translocating adenosine triphosphatase (H(+)-ATPase) and a 50-kD protein. The 69-kD subunit is encoded by the 5' and
Patricia M. Kane +8 more
semanticscholar +1 more source
Deoxyuridine triphosphatase in human hepatoma
International Journal of Biochemistry, 19941. 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
openaire +3 more sources
Structure of the Vacuolar Adenosine Triphosphatases
Cell Biochemistry and Biophysics, 2001Vacuolar 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.
openaire +3 more sources
Adenosine triphosphatase distribution in mammary tissue [PDF]
The 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
openaire +2 more sources
Energetics and mechanism of actomyosin adenosine triphosphatase.
Biochemistry, 1976Rate constants were determined for the reaction of actin with subfragment 1 (S1), S1-product complex, heavy meromyosin (HMM), and HMM-products complex for a range of temperatures, pH's, and ionic strengths. For actin concentrations up to 10 muM, the rate
H. White, E. Taylor
semanticscholar +1 more source
Adenosine Triphosphatase Activity of Mycoplasma Membranes [PDF]
Journal of Bacteriology, 1966 Rottem, Shlomo (Hebrew University, Jerusalem, Israel), and Shmuel Razin . Adenosine triphosphatase activity of mycoplasma membranes. J. Bacteriol. 92: 714–722. 1966.—Adenosine triphosphatase activity of Mycoplasma laidlawii, M. gallisepticum , and
Shlomo Rottem, Shmuel Razin
openaire +2 more sources