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rdf:type |
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|
lifeskim:mentions |
|
|
pubmed:issue |
2
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pubmed:dateCreated |
1977-3-21
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pubmed:abstractText |
L-Leucine-pyruvate transaminase (mol. wt. 70 000) in Gluconobactersuboxydans synthesized during nitrogen starvation contained a labile form which changed to the stable one later. The labile enzyme (mol. wt. 70 000) dissocated to the two proteinaceous components: a cationic one (mol. wt. 10 000--20 000) and an anionic one (mol. wt. 50 000--60 000), during column chromatography on DEAE-cellulose. The enzyme activity was reconstructed when they were mixed. The reconstructed enzyme had almost the same molecular size and enzymatic properties as the labile and the native stable enzymes.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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|
pubmed:issn |
0006-3002
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
8
|
|
pubmed:volume |
452
|
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
621-4
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|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
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pubmed:year |
1976
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|
pubmed:articleTitle |
Resolution and complementation of the labile L-leucine-pyruvate transaminase. An intermediate during enzyme formation under nitrogen starvation in Gluconobacter suboxydans.
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pubmed:publicationType |
Journal Article
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