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  The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin

Mannherz, H. G., Goody, R. S., Konrad, M., & Nowak, E. (1980). The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. European Journal of Biochemistry, 104(2), 367-379. doi:10.1111/j.1432-1033.1980.tb04437.x.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0004-B6C1-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0004-B6C2-3
Genre: Journal Article

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EurJBiochem_104_1980_367.pdf (Any fulltext), 2MB
 
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https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1980.tb04437.x (Any fulltext)
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 Creators:
Mannherz, Hans Georg1, 2, Author           
Goody, Roger S.1, 2, 3, Author           
Konrad , Manfred, Author
Nowak, Ewa, Author
Affiliations:
1Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Abt. III: Strukturbiochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_2040307              

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 Abstract: The rate of exchange of actin-bound nucleotide is decreased by a factor of about 20 when actin is complexed with DNAase I without affecting the binding constant of calcium for actin. Binding constants of DNAase I to monomeric and filamentous actin were determined to be 5 X 10(8) M-1 and 1.2 X 10(4) M-1 respectively. The depolymerisation of F-actin by DNAase I appears to be due to a shift in the G-F equilibrium of actin by DNAase I. Inhibition of the DNA-degrading activity of DNAase I by G-actin is of the partially competitive type.

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Language(s): eng - English
 Dates: 1979-08-022005-03-031980-03
 Publication Status: Issued
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1432-1033.1980.tb04437.x
URI: 10.1111/j.1432-1033.1980.tb04437.x
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 104 (2) Sequence Number: - Start / End Page: 367 - 379 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040