Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1986-2-13
|
pubmed:abstractText |
Cells of Euglena gracilis Klebs strain z Pringsheim had high NADP-dependent glutamate dehydrogenase activity when grown on glutamate as nitrogen source but activity was completely repressed in cells grown on ammonium (NH4+). A 120-fold purification of NADPH-glutamate dehydrogenase (subunit Mr = 45 000) was achieved from glutamate-grown cells by affinity chromatography on blue Sepharose CL-6B. Antisera raised against the homogeneously pure protein were used to demonstrate that increase in NADPH-glutamate dehydrogenase activity on transfer from NH4+ to glutamate medium resulted from an increase in the amount of protein. Glutamate NH4+-grown cells were labelled with L-[35S]methionine and anti-(NADPH-glutamate dehydrogenase) used to immunoprecipitate the dehydrogenase from cell extracts. NADPH-glutamate dehydrogenase protein was detected in glutamate-grown but not NH4+-grown cells. Anti-(NADPH-glutamate dehydrogenase) was used to detect NADPH-glutamate dehydrogenase resulting from the translation of total polyadenylated RNA from Euglena in a cell-free rabbit reticulocyte lysate system. NADPH-glutamate dehydrogenase mRNA was present in glutamate NH4+-grown cells, there being no apparent difference in mRNA abundance between cells showing a tenfold difference in NADPH-glutamate dehydrogenase specific activity. These results indicate that the synthesis of this dehydrogenase is regulated primarily at the post-transcriptional level.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Dehydrogenase (NADP ),
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-2956
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
153
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
573-8
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:2866958-Culture Media,
pubmed-meshheading:2866958-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2866958-Euglena gracilis,
pubmed-meshheading:2866958-Glutamate Dehydrogenase,
pubmed-meshheading:2866958-Glutamate Dehydrogenase (NADP+),
pubmed-meshheading:2866958-Immunochemistry,
pubmed-meshheading:2866958-Methionine,
pubmed-meshheading:2866958-Nitrogen,
pubmed-meshheading:2866958-Photofluorography,
pubmed-meshheading:2866958-Poly A,
pubmed-meshheading:2866958-Protein Biosynthesis,
pubmed-meshheading:2866958-RNA, Messenger,
pubmed-meshheading:2866958-RNA Processing, Post-Transcriptional
|
pubmed:year |
1985
|
pubmed:articleTitle |
Glutamate dehydrogenase (NADP-dependent) mRNA in relation to enzyme synthesis in Euglena gracilis. Evidence for post-transcriptional control.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|