Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1978-10-25
|
| pubmed:abstractText |
Membranes from a mutant strain of Escherichia coli K12 carrying the uncD409 allele were washed in low-ionic-strength buffers in the presence or absence of the proteinase inhibitor p-aminobenzamidine. Unlike membranes from a normal strain, those from strain AN463 (uncD409) did not become proton-permeable, as judged by NADH-induced atebrinfluorescence quenching, when the membranes were washed in the absence of p-aminobenzamide. Furthermore, ATP-dependent atebrin-fluorscence quenching in such washed membranes could not be reconstituted by the addition of solubilized Mg2+-stimulated adenosine triphosphatase preparations. The examination by two-dimensional polyacrylamide-gel electrophoresis of the polypeptide composition of the washed membranes from strain AN463 (uncD409) indicated the presence of a polypeptide of similar molecular weight to the normal beta-subunit of the Mg2+-stimulated adenosine triphosphatase, but with an altered isoelectric point. Both the normal and abnormal beta-subunits were identified in membranes prepared from a partial diploid strain carrying both the unc+ and uncD409 alleles. It is concluded that the uncD gene codes for the beta-subunit of the Mg2+-stimulated adenosine triphosphatase.
|
| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-1267736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-127796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-128353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-13475269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-141275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-141927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-145433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-148275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-236308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-237462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-4145024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-4192611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-4269101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-4343963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/150841-773363
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0264-6021
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
172
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
523-31
|
| pubmed:dateRevised |
2009-11-18
|
| pubmed:meshHeading | |
| pubmed:year |
1978
|
| pubmed:articleTitle |
Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered beta-subunit of the magnesium ion-stimulated adenosine triphosphatase.
|
| pubmed:publicationType |
Journal Article,
In Vitro
|