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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1995-5-9
|
| pubmed:abstractText |
It has previously been shown that baker's yeast trans ketolase has no intersubunit disulfide bonds and is able to dissociate reversibly into subunits at a low apoprotein concentration in solution. By contrast, in the present work it was found that in the molecule of transketolase C (a newly discovered form of the enzyme) subunits are bound to each other by disulfide bonds.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
1039-9712
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
34
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1049-54
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1994
|
| pubmed:articleTitle |
Intersubunit disulfide bonds in the molecule of baker's yeast transketolase.
|
| pubmed:affiliation |
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|