Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-9-20
pubmed:abstractText
Methylenetetrahydromethanopterin reductase from metanogenic archaebacteria catalyzes the reversible reduction of N5,N10-methylenetetrahydromethanopterin to N5-methyltetrahydromethanopterin with reduced coenzyme F420 as electron donor. The enzyme is involved in methane formation from CO2 and in methanol disproportionation to CO2 and CH4. We report here that the reductase from Methanobacterium thermoautotrophicum specifically binds to Blue Sepharose CL-6B. Binding was competitive with coenzyme F420 rather than with NAD, NADP, FAD, FMN, AMP, ADP and ATP. The reductase could also be desorbed with salt. Based on this property an affinity chromatographic procedure for the purification of the enzyme was developed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
59-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B.
pubmed:affiliation
Fachbereich Biologie, Philipps-Universität, Marburg/Lahn, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't