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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 |
1972-4-18
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pubmed:abstractText |
A Bacillus subtilis mutant having a phenotype manifesting reduced extracellular proteolytic activity was investigated. An extracellular protein was isolated and shown by fingerprint analysis to be a fragment of the wild-type enzyme. By using previously established molecular weights for the wild-type enzyme (2.9 x 10(4)) and the two polypeptide chains derived from it (1.4 x 10(4) each), with the amino acid analysis and fingerprints of both wild-type and mutant proteins, a molecular weight of 1.57 x 10(4) was assigned to the mutant protein. (32)P-diisopropylphosphate labeling of the mutant protein showed only 1 in 53 molecules to be functional. Thin-layer chromatography on Sephadex G-75 demonstrated that the active molecules were separable from the bulk of the isolated protein and had the same mobility as the wild-type enzyme. Fingerprints of tryptic digests of (32)P-diisopropylphosphate-labeled wild-type and mutant proteins showed that the labeled peptides had identical characteristics.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-13560404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14239476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14240539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14253470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14253471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14404843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14882323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-16590310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-4896351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-5107857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-5266165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4621679-5579943
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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 |
Feb
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
109
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
575-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:4621679-Amino Acids,
pubmed-meshheading:4621679-Autoanalysis,
pubmed-meshheading:4621679-Bacillus subtilis,
pubmed-meshheading:4621679-Bacterial Proteins,
pubmed-meshheading:4621679-Carbon Isotopes,
pubmed-meshheading:4621679-Cell-Free System,
pubmed-meshheading:4621679-Chromatography, Thin Layer,
pubmed-meshheading:4621679-Electrophoresis, Disc,
pubmed-meshheading:4621679-Genetics, Microbial,
pubmed-meshheading:4621679-Hydrogen-Ion Concentration,
pubmed-meshheading:4621679-Molecular Weight,
pubmed-meshheading:4621679-Mutation,
pubmed-meshheading:4621679-Peptide Hydrolases,
pubmed-meshheading:4621679-Peptides,
pubmed-meshheading:4621679-Phenotype,
pubmed-meshheading:4621679-Phosphates,
pubmed-meshheading:4621679-Phosphorus Isotopes,
pubmed-meshheading:4621679-Trypsin,
pubmed-meshheading:4621679-Ultracentrifugation
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pubmed:year |
1972
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pubmed:articleTitle |
Analysis of a Bacillus subtilis proteinase mutant.
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pubmed:publicationType |
Journal Article
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