Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenosine triphosphatase (ATPase) was studied in tissue homogenates and subcellular fractions derived from human cadaver kidneys maintained in an organ preservation unit for transplantation. The activity of ouabain-sensitive ATPase was highest in the medulla, intermediate in the cortex and lowest in the papilla, The cortical enzyme activity diminished with time during maintenance perfusion of the kidneys. Similar concentrations of K+, Na+, Mg++, ATP and MgATP were required for half-maximal rates of ouabain-sensitive ATPase activity from the cortex or the medulla. The sensitivity of the enzyme to ouabain from both parts of the kidney was similar. K+ antagonized inhibition of the enzyme by ouabain. Chlormerodrin, mersalyl, mercaptomerin and ethacrynic acid were inhibitors of the enzyme.
 ...
PMID:Ouabain-sensitive adenosine triphosphatase from human kidneys. 12 73

Adenosine triphosphatase (ATPase) was studied in tissue homogenates and subcellular fractions derived from human cadaver kidneys maintained in an organ preservation unit for transplantation. The activity of ouabain-sensitive ATPase was highest in the medulla, intermediate in the cortex and lowest in the papilla. The cortical enzyme activity diminished with time during maintenance perfusion of the kidneys. Similar concentrations of K+, Na+, Mg++, ATP and MgATP were required for half-maximal rates of ouabain-sensitive ATPase activity from the cortex or the medulla. The sensitivity of the enzyme to ouabain from both parts of the kidney was similar. K+ antagonized inhibition of the enzyme by ouabain. Chlormerodrin, mersalyl, mercaptomerin and ethacrynic acid were inhibitors of the enzyme.
 ...
PMID:Oubain-sensitive adenosine triphosphatase from human kidneys. 12 74

A new ATP-dependent, casein-degrading proteolytic complex has been identified and partially purified from Escherichia coli. The proteolytic complex can be isolated from wild-type cells as well as from mutants in which the gene for the ATP-dependent Lon protease is deleted. The complex consists of at least two components (components I and II) that can be separated from each other (and from wild-type Lon protease) by phosphocellulose chromatography. Neither component has casein-degrading activity when added separately to assay solutions with or without ATP. Both components must be present simultaneously for casein degradation to occur. Of the nucleotides tested, only ATP activates the proteolytic complex, and the ATP must be present continuously for degradation to occur. Component II copurifies with an ATPase activity and binds to a Type 4 ATP affinity column. ATP protects component II from heat inactivation, suggesting that component II interacts with ATP. Proteolysis was not inhibited by any serine protease inhibitors but was inhibited by reagents such as the organomercurial Neohydrin and N-ethylmaleimide, which react with sulfhydryl groups. Our data provide convincing evidence that E. coli possesses a previously undescribed proteolytic system composed of at least two complementary components and absolutely dependent on ATP.
 ...
PMID:A multiple-component, ATP-dependent protease from Escherichia coli. 354 8