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Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate

Mockrin, Stephen C., Korn, Edward D.·1980·Biochemistry

Abstract

A sevenfold 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 x 10(-4) to 1.3 x 10(-2) S-1, at 25 degrees 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 x 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+.

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Metadata

Authors
Mockrin, S. C., & Korn, E. D.
Venue
Biochemistry
Published
1980-11-11
Volume
19
Issue
23
Pages
5359-5362
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2054446803
Cited by
277
References
0
FWCI
1.80
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate. https://app.cochat.ai/papers/10.1021/bi00564a033
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Mockrin, S. C., & Korn, E. D. (1980). Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry. https://doi.org/10.1021/bi00564a033

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