ACANTHAMOEBA PROFILIN INTERACTS WITH G-ACTIN TO INCREASE THE RATE OF EXCHANGE OF ACTIN-BOUND ADENOSINE 5'-TRIPHOSPHATE
ACANTHAMOEBA PROFILIN INTERACTS WITH G-ACTIN TO INCREASE THE RATE OF EXCHANGE OF ACTIN-BOUND ADENOSINE 5'-TRIPHOSPHATE
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DOI:
10.1021/bi00564a033
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发表时间:
1980-01-01
期刊:
影响因子:
2.9
通讯作者:
KORN, ED
中科院分区:
文献类型:
--
作者:
MOCKRIN, SC;KORN, ED
A 7-fold molar excess of Acanthamoeba profilin, a 12,000-dalton protein that inhibits actin polymerization, increases the rate of exchange of ATP bound to G-actin with ATP in solution about 17-fold, i.e., from 7.7 .times. 10-4 to 1.3 .times. 10-2 s-1, at 25.degree. C, 0.033 mM Ca2+ and 0.1 mM ATP, pH 7.5. Detailed analysis of the equilibrium isotope-exchange data shows that profilin and actin form a 1:1 complex with KD = 4.7 .times. 10-5 M and that the binding of profilin to actin is rapid and reversible. The actin-profilin complex binds 1 mol of ATP/mol, as does G-actin. Profilin does not interact with ATP or Ca2+.