| pubmed-article:8061621 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0004591 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0036734 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0018837 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C0311417 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C1622131 | lld:lifeskim |
| pubmed-article:8061621 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:8061621 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8061621 | pubmed:dateCreated | 1994-9-22 | lld:pubmed |
| pubmed-article:8061621 | pubmed:abstractText | The intracellular Ca(2+)-dependent serine proteinase (ISP1) activity in the cytoplasm of nongrowing Bacillus megaterium incubated in a sporulation medium was determined at 35 degrees C and at temperatures decreasing the sporulation frequency (42 degrees C) or suppressing sporulation (43.5 degrees C). The enzyme in the crude cytoplasmic fraction was partially inhibited by a loosely bound inhibitor(s) because the ISP1 activity rose after protein fractionation by HPLC. Temperature shift-up or osmotic stress applied at 35 degrees C increased the development of the ISP1 activity several times. The increase was caused at least partially by the synthesis of the enzyme protein, as proved by SDS-PAGE and immunoblotting of the cytoplasm. This enzyme thus probably belongs among heat-shock proteins. | lld:pubmed |
| pubmed-article:8061621 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8061621 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8061621 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8061621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8061621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8061621 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8061621 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8061621 | pubmed:issn | 1039-9712 | lld:pubmed |
| pubmed-article:8061621 | pubmed:author | pubmed-author:ChaloupkaJJ | lld:pubmed |
| pubmed-article:8061621 | pubmed:author | pubmed-author:KucerováHH | lld:pubmed |
| pubmed-article:8061621 | pubmed:author | pubmed-author:VáchováLL | lld:pubmed |
| pubmed-article:8061621 | pubmed:author | pubmed-author:BenesováJJ | lld:pubmed |
| pubmed-article:8061621 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8061621 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8061621 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8061621 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8061621 | pubmed:pagination | 1049-57 | lld:pubmed |
| pubmed-article:8061621 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:meshHeading | pubmed-meshheading:8061621-... | lld:pubmed |
| pubmed-article:8061621 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8061621 | pubmed:articleTitle | Heat and osmotic stress enhance the development of cytoplasmic serine proteinase activity in sporulating Bacillus megaterium. | lld:pubmed |
| pubmed-article:8061621 | pubmed:affiliation | Department of Molecular and Cellular Microbiology, Academy of Sciences of the Czech Republic, Prague. | lld:pubmed |
| pubmed-article:8061621 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8061621 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
