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A protease from Legionella pneumophila with cytotoxic and dermal ulcerative activity (1986)

Rosenfeld, J.S. ; Kueppers, F. ; Newkirk, T. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 37 (1986), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract Culture supernatants of Legionella pneumophila, Philadelphia 1, were found to have proteolytic activity, as well as a nondialyzable, heat-labile cytotoxin for Chinese hamster ovary (CHO) cells, and a factor which caused hemorrhagic dermal ulceration when injected intradermally into mice. A protease was purified from culture supernates by filtration on Sephacryl S-200 followed by chromatography on DEAE cellulose. Proteolytic activity had a pH optimum of 5.5, and migrated as two bands in PAGE, with molecular weights of 42 and 31 kDa. CHO cell cytotoxic, dermal ulcerative, and proteolytic activities copurified. The results are consistent with the same protein being responsible for these activities.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01765.x

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Rhamnolipid from Pseudomonas aeruginosa inactivates mammalian tracheal ciliary axonemes (1986)

Hastie, A. T. ; Hingley, S. T. ; Higgins, M. L. ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 6 (1986), S. 502-509

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ISSN: 0886-1544

Keywords: respiratory cilia ; dynein ; ATPase ; cystic fibrosis ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Isolated ciliary axonemes from pig trachea were exposed to increasing concentrations of purified Pseudomonas aeruginosa rhamnolipid. This is a defined ciliary system allowing observation of direct impairment of functional axonemes. Axonemal motility and ATPase activity were decreased in proportion to rhamnolipid concentrations. ATPase-associated proteins observed in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and dynein arms seen in ultrastructural cross sections progressively disappeared from axonemes with exposure to rhamnolipid. These four independent measures establish that the rhamnolipid removes the ATPase-containing outer dynein arms from the ciliary axoneme, thereby rendering the axoneme immotile.

Additional Material: 4 Ill.