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Membrane proteins and squalene-hydrosqualene profile in methanoarchaeon Methanothermobacter thermautotrophicus resistant to N,N'-dicyclohexylcarbodiimide
Zuzana Nováková, Stanislav Šurín, Jaroslav Blaško, Alan Majerník, Peter Šmigáň
Jazyk angličtina Země Česko
- MeSH
- antibiotická rezistence MeSH
- buněčná membrána metabolismus MeSH
- dicyklohexylkarbodiimid farmakologie metabolismus MeSH
- energetický metabolismus MeSH
- membránové proteiny genetika metabolismus MeSH
- Methanobacteriaceae genetika metabolismus účinky léků MeSH
- mutace MeSH
- skvalen chemie metabolismus MeSH
The biochemical basis of a defective bioenergetic system was attempted to be determined in N,N'-dicyclohexylcarbodiimide (DCCD)-resistant mutant of Methanothermobacter thermautotrophicus. Components participating in the maintenance of methanoarchaeal membrane structure and function, such as the composition of the mixture of squalene and its hydrosqualene derivatives and also properties of membrane-associated proteins were compared in wild-type and mutant cells. The impairment of the bioenergetic system in DCCD-resistant mutant was detectable in the membrane-protein profile; it was also accompanied by changes in proportions of squalene-hydrosqualenes.
Lit.: 18
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- 20111210124703.0
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- 081209s2008 xr e eng||
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- $2 doi $a 10.1007/s12223-008-0034-x
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- $a eng
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- $a xr
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- $a Nováková, Zuzana $7 xx0117642
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- 314 __
- $a Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Ivanka pri Dunaji
- 504 __
- $a Lit.: 18
- 520 9_
- $a The biochemical basis of a defective bioenergetic system was attempted to be determined in N,N'-dicyclohexylcarbodiimide (DCCD)-resistant mutant of Methanothermobacter thermautotrophicus. Components participating in the maintenance of methanoarchaeal membrane structure and function, such as the composition of the mixture of squalene and its hydrosqualene derivatives and also properties of membrane-associated proteins were compared in wild-type and mutant cells. The impairment of the bioenergetic system in DCCD-resistant mutant was detectable in the membrane-protein profile; it was also accompanied by changes in proportions of squalene-hydrosqualenes.
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