Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1971-7-20
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
233
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-16
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:4252903-Adenosine Triphosphatases, pubmed-meshheading:4252903-Adenosine Triphosphate, pubmed-meshheading:4252903-Animals, pubmed-meshheading:4252903-Binding Sites, pubmed-meshheading:4252903-Brain, pubmed-meshheading:4252903-Cattle, pubmed-meshheading:4252903-Chemical Phenomena, pubmed-meshheading:4252903-Chemistry, pubmed-meshheading:4252903-Cold Temperature, pubmed-meshheading:4252903-Dialysis, pubmed-meshheading:4252903-Edetic Acid, pubmed-meshheading:4252903-Enzyme Activation, pubmed-meshheading:4252903-Hot Temperature, pubmed-meshheading:4252903-Magnesium, pubmed-meshheading:4252903-Microsomes, pubmed-meshheading:4252903-Phosphorus Isotopes, pubmed-meshheading:4252903-Potassium, pubmed-meshheading:4252903-Protein Binding, pubmed-meshheading:4252903-Protein Denaturation, pubmed-meshheading:4252903-Sodium
pubmed:year
1971
pubmed:articleTitle
Binding of ATP to brain microsomal ATPase. Determination of the ATP-binding capacity and the dissociation constant of the enzyme-ATP complex as a function of K+ concentration.
pubmed:publicationType
Journal Article