Abstract:
:Plasma membrane H(+)-ATPase of the yeast Saccharomyces cerevisiae was isolated and purified in its two forms, the activated A-ATPase from glucose-metabolizing cells, and the basal-level B-ATPase from cells with endogenous metabolism only. Using two-dimensional gel electrophoretic analysis, we showed that both enzyme preparations are actually mixtures of the non-active, i.e. non-phosphorylated, and the active, i.e. phosphorylated, forms of the enzyme. Previous deliberations suggesting that the B-ATPase displays some activity which is lower than that of A-ATPase were apparently wrong. It seems that, molecularly speaking, the B-form is actually not active at all, and what activity we measure in our preparation is due to an admixture of the true active form (A-form). Fourier transform infrared spectroscopic study of the secondary structure and particularly thermal denaturation data suggest the possibility that the two enzyme forms interact to form complexes less stable than the single forms. On the whole then, there apparently is a different ratio of the active and inactive forms and/or complexes between the two forms present in all enzyme preparations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lapathitis G,Tanfani F,Kotyk A,Bertoli Edoi
10.1016/s0014-5793(01)02793-4keywords:
subject
Has Abstractpub_date
2001-09-07 00:00:00pages
155-8issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02793-4journal_volume
505pub_type
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