Linked Life Data

6986368

Source:http://linkedlifedata.com/resource/pubmed/id/6986368

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1980-4-23
pubmed:abstractText
A deoxyadenosylcobalamin-dependent ribonucleoside diphosphate reductase has been purified to homogeneity from cell free extracts of Corynebacterium nephridii. Ion exchange chromatography of th extract on DEAE-Sephadex and DEAE-Bio-Gel A, followed by affinity chromatography on dGTP-Sepharose, yielded two forms of the reductase. The first reductase, which was weakly bound to the affinity column, was eluted with 0.1 M citrate buffer, pH 6.5, while the second, more tightly bound form required 2 M urea for its elution. The weakly bound form is homogeneous as judged by gel filtration, equilibrium sedimentation, and polyacrylamide gel electrophoresis. This enzyme is a dimeric protein with a molecular weight of 196,000, composed of two identical or very similar subunits with molecular weights of 100,000. The second protein appears to be a polymeric form of the reductase. Both forms of the enzyme catalyze the reduction of the four common ribonucleoside diphosphates as well as the hydrogen exchange between adenosylcobalamin and the solvent. The ribonucleoside diphosphate reductase system of C. nephridii appears to be intermediate between the more "primitive" adenosylcobalamin-dependent reductase system of Lactobacillus leichmannii and the more "advanced" nonheme iron system of Escherichia coli.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1273-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The purification and characterization of an adenosylcobalamin-dependent ribonucleoside diphosphate reductase from Corynebacterium nephridii.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.