Source:http://linkedlifedata.com/resource/pubmed/id/13870521
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1962-12-1
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pubmed:abstractText |
The kinetics of beta-galactosidase induction in E. coli ML 3 have been studied. Following addition of inducer, the rate of enzyme synthesis accelerates from the uninduced to a steady-state rate. At saturating concentration of inducer the time constant (T(c)) for this process is 2.5 to 3 minutes. With decreasing inducer concentration (I), increasing time constants are observed. I/I + K' approximates I/T(c). The steady-state rate of beta-galactosidase synthesis is approximated by I(2)/I(2) + K(2). K' and K have been estimated for IPTG and TMG. The kinetics of beta-galactosidase production after the removal of inducer by dilution or after the addition of glucose have been investigated. A transition time of 2.5 to 3 minutes is observed before enzyme synthesis slows or stops. These results are consistent with the hypothesis that the enzyme-forming unit is unstable.
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pubmed:commentsCorrections | |
pubmed:keyword | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
OM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3495
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
639-47
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading | |
pubmed:year |
1961
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pubmed:articleTitle |
Kinetic studies of beta-galactosidase induction.
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pubmed:publicationType |
Journal Article
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