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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1983-12-20
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pubmed:abstractText |
Extracellular penicillinases produced by Bacillus licheniformis ATCC 9945A and Bacillus subtilis from the same structural gene, penP, were compared. The two strains secreted the same exo-large penicillinase (mol. wt, 305000; isoelectric point, pI = 5.00-5.04; NH2-terminal amino acid, Ser). In contrast, the exo-small enzyme from Bacillus subtilis (mol. wt, 29500; pI = 5.00-5.04; NH2-terminal amino acid, Glu or Asn) was slightly different from that of Bacillus licheniformis (mol. wt, 29500; pI = 5.13; NH2-terminal amino acid, Lys). The difference in the NH2-terminal residue is most probably due to differences in degradation by host-specific proteolytic enzymes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1287
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
129
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2621-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6415232-Amino Acid Sequence,
pubmed-meshheading:6415232-Bacillus,
pubmed-meshheading:6415232-Bacillus subtilis,
pubmed-meshheading:6415232-Base Sequence,
pubmed-meshheading:6415232-Chromatography, Thin Layer,
pubmed-meshheading:6415232-Chromosome Mapping,
pubmed-meshheading:6415232-Genes,
pubmed-meshheading:6415232-Genes, Bacterial,
pubmed-meshheading:6415232-Isoelectric Focusing,
pubmed-meshheading:6415232-Molecular Weight,
pubmed-meshheading:6415232-Penicillinase
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pubmed:year |
1983
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pubmed:articleTitle |
Comparative studies on extracellular penicillinases of the same structural gene, penP, expressed in Bacillus licheniformis and Bacillus subtilis.
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pubmed:publicationType |
Journal Article,
Comparative Study
|