Abstract:
:The ATP synthase of the yeast Saccharomyces cerevisiae is composed of 20 different subunits whose primary structure is known. The organization of proteins that constitute the membranous domain is now under investigation. Cysteine insertions combined with the use of nonpermeant maleimide reagents and cross-linking reagents showing different lengths and specificity contribute to the knowledge of the location of the N- and C-termini of the subunits involved in the stator of the enzyme and their organization. This review summarizes data on yeast ATP synthase obtained in our laboratory since 1980.
journal_name
J Bioenerg Biomembrjournal_title
Journal of bioenergetics and biomembranesauthors
Velours J,Arselin Gdoi
10.1023/a:1005580020547keywords:
subject
Has Abstractpub_date
2000-08-01 00:00:00pages
383-90issue
4eissn
0145-479Xissn
1573-6881journal_volume
32pub_type
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journal_title:Journal of bioenergetics and biomembranes
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journal_title:Journal of bioenergetics and biomembranes
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更新日期:2012-06-01 00:00:00
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更新日期:2007-04-01 00:00:00
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更新日期:2003-06-01 00:00:00
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更新日期:2008-04-01 00:00:00
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journal_title:Journal of bioenergetics and biomembranes
pub_type: 杂志文章,评审
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journal_title:Journal of bioenergetics and biomembranes
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更新日期:1980-12-01 00:00:00
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journal_title:Journal of bioenergetics and biomembranes
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更新日期:2010-06-01 00:00:00
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