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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1976-9-1
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pubmed:abstractText |
Aminoethylated beta-galactosidase from Escherichia coli was cleaved by CNBr. The fragment C4a was purified by gel filtration and ion-exchange chromatography. The molecular weight of the fragment C4a was determined to be 9000 +/- 600. The N-terminal amino acid was found to be isoleucine. Qualitative examination of homogeneity was carried out by disc-gel electrophoresis. The fragment C4a was shown to be active as an alpha donor in complementation of beta-galactosidase activity in vitro with E. coli mutant M15, which has a deletion in the alpha region of the z gene. The molecular weights of complementable fractions from mutant M15 were found to be 123 000 +/- 2500 and 507 000 +/- 11 000, and of the complemented enzyme 522 500 +/- 11 400.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-13135413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-13319283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-13628682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-13638015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-14084623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-14304855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-14304856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4861258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4868117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4919959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4920424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4922497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-4944355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-5339869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-5417264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-5780484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/779770-6029938
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
155
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
209-16
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:779770-Amino Acids,
pubmed-meshheading:779770-Ammonium Sulfate,
pubmed-meshheading:779770-Cyanogen Bromide,
pubmed-meshheading:779770-Enzyme Activation,
pubmed-meshheading:779770-Escherichia coli,
pubmed-meshheading:779770-Galactosidases,
pubmed-meshheading:779770-Genetic Complementation Test,
pubmed-meshheading:779770-Isoleucine,
pubmed-meshheading:779770-Models, Biological,
pubmed-meshheading:779770-Molecular Weight,
pubmed-meshheading:779770-Mutation,
pubmed-meshheading:779770-Peptide Fragments
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pubmed:year |
1976
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pubmed:articleTitle |
A cyanogen bromide fragment of beta-galactosidase from Escherichia coli with alpha-donor activity in complementation of the enzyme from mutant M15.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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