Linked Life Data

8061621

Source:http://linkedlifedata.com/resource/pubmed/id/8061621

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-9-22
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1049-57
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Heat and osmotic stress enhance the development of cytoplasmic serine proteinase activity in sporulating Bacillus megaterium.
pubmed:affiliation
Department of Molecular and Cellular Microbiology, Academy of Sciences of the Czech Republic, Prague.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't