Abstract:
:F1-ATPase inhibitor was purified from yeast, Saccharomyces cerevisiae. The purified inhibitor blocked ATPase activity in the presence of ATP and Mg2+ by forming a latent equimolar enzyme-inhibitor complex with ATP and ADP newly bound to loose sites on the enzyme. A small portion of externally added ATP was hydrolyzed before the latent complex was formed but the hydrolysis was not directly related to the complex formation. Newly bound ATP tended to be converted to ADP when the ATP concentration of the medium was low. ATP tightly bound to the enzyme was not directly involved in formation of the complex. The complex was fairly stable in the presence of excess inhibitor and ATP but at a high concentration of the enzyme (10(-5) M), the inhibition was not complete, although only about 0.03% of the original activity remained unblocked.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Hashimoto T,Negawa Y,Tagawa Kdoi
10.1093/oxfordjournals.jbchem.a133567subject
Has Abstractpub_date
1981-10-01 00:00:00pages
1151-7issue
4eissn
0021-924Xissn
1756-2651journal_volume
90pub_type
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