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  The sulfoxide of thymosin β4 almost lacks the polymerization-inhibiting capacity for actin

Heintz, D., Reichert, A. J. J., Mihelic−Rapp, M., Stoeva, S., Voelter, W. J., & Faulstich, H. (1994). The sulfoxide of thymosin β4 almost lacks the polymerization-inhibiting capacity for actin. European Journal of Biochemistry, 223(2), 345-350. doi:10.1111/j.1432-1033.1994.tb19000.x.

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Heintz, Daniela1, Author              
Reichert, Andreas J. J.2, Author              
Mihelic−Rapp, Mirna, Author
Stoeva, Stanka, Author
Voelter, Wolfgang J., Author
Faulstich, Heinz2, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

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 Abstract: Thymosin β4 (Tβ4), a peptide of 43 amino acids, binds to actin monomers and inhibits filament formation. In preparations of Tβ4 from bovine lung tissue, the peptide is accompanied by a derivative in which the methionine residue in position 6 is replaced by its sulfoxide. Tβ4 sulfoxide inhibits actin polymerization to an extent approximately 20-times less than Tβ4. While an equimolar amount of Tβ4 prevented actin polymerization almost completely, polymerization with the corresponding amount of the sulfoxide proceeded in a manner similar to that of pure actin, except for a slight retardation. We showed that the decrease in the inhibitory activity is reflected by a 20-times lower affinity to actin. Interestingly, under non-polymerizing conditions, the affinity of Tβ4 sulfoxide for actin is as high as that of Tβ4 (approximately 1 μM). In accordance with this, no differences were found between Tβ4 and the sulfoxide in cross-linking experiments with the monomer, where both forms of the peptide yielded similar amounts of a 47-kDa band representing conjugates of actin and β-thymosin, as proved by Western-blotting analysis. Likewise, both, Tβ4 and the sulfoxide retarded the exchange of G-actin-bound nucleotide to similar extents. Although the sulfoxide is presumably a product of autoxidation, it is attractive to speculate that oxidation of the methionine residue in Tβ4 may represent a regulatory switch for starting filament formation in non-muscle cells.

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Language(s): eng - English
 Dates: 1994-03-112005-03-031994-07
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665151
DOI: 10.1111/j.1432-1033.1994.tb19000.x
Other: 6917
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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: 223 (2) Sequence Number: - Start / End Page: 345 - 350 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040