Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1979-12-20
|
pubmed:abstractText |
Bovine liver dihydropyrimidine amidohydrolase (EC 3.5.2.2) has been subjected to atomic absorption analysis. Three different preparations of homogeneous enzyme indicated that the enzyme contains 4.3 +/- 0.3 g atoms of Zn2+ per mol of enzyme or 1.1 g atoms of Zn2+ per subunit. No Co2+, Mn2+, Mg2+ or Cd2+ was detected. Exhaustive dialysis against either o-phenanthroline or EDTA did not reduce enzyme activity; however, prolonged incubation with dipicolinic acid resulted in inactivation which can be reversed by either Zn2+ or Co2+ but not Mg2+.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
12
|
pubmed:volume |
570
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
213-4
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:486503-Amidohydrolases,
pubmed-meshheading:486503-Animals,
pubmed-meshheading:486503-Cattle,
pubmed-meshheading:486503-Liver,
pubmed-meshheading:486503-Metalloproteins,
pubmed-meshheading:486503-Spectrophotometry, Atomic,
pubmed-meshheading:486503-Uracil,
pubmed-meshheading:486503-Zinc
|
pubmed:year |
1979
|
pubmed:articleTitle |
Dihydropyrimidine amidohydrolase is a zinc metalloenzyme.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|