| pubmed-article:8405954 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0221099 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0051581 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:8405954 | lifeskim:mentions | umls-concept:C0017724 | lld:lifeskim |
| pubmed-article:8405954 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8405954 | pubmed:dateCreated | 1993-11-22 | lld:pubmed |
| pubmed-article:8405954 | pubmed:abstractText | The purified autolytic endo-beta-N-acetylglucosaminidase of Bacillus subtilis AC327 was cleaved with cyanogen bromide, and the N-terminal amino acid sequence of one of the peptide fragments was determined. Then, a DNA fragment containing a part of the glucosaminidase gene was cloned into Escherichia coli JM109 using synthetic oligonucleotides as probes whose sequences had been deduced from the N-terminal amino acid sequence. Zymographic analysis showed that the resultant glucosaminidase-deficient strain lacked a 35-kDa lytic band in addition to a 90-kDa lytic one corresponding to the glucosaminidase. A double mutant strain deficient in the major two autolysins (amidase and glucosaminidase) exhibited greatly impaired motility on a swarm plate whereas the single mutant strains were motile. | lld:pubmed |
| pubmed-article:8405954 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8405954 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8405954 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8405954 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8405954 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8405954 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8405954 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8405954 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8405954 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:8405954 | pubmed:author | pubmed-author:KurodaAA | lld:pubmed |
| pubmed-article:8405954 | pubmed:author | pubmed-author:SekiguchiJJ | lld:pubmed |
| pubmed-article:8405954 | pubmed:author | pubmed-author:RashidM HMH | lld:pubmed |
| pubmed-article:8405954 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8405954 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8405954 | pubmed:volume | 112 | lld:pubmed |
| pubmed-article:8405954 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8405954 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8405954 | pubmed:pagination | 135-40 | lld:pubmed |
| pubmed-article:8405954 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:meshHeading | pubmed-meshheading:8405954-... | lld:pubmed |
| pubmed-article:8405954 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8405954 | pubmed:articleTitle | Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility. | lld:pubmed |
| pubmed-article:8405954 | pubmed:affiliation | Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan. | lld:pubmed |
| pubmed-article:8405954 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8405954 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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