| Literature DB >> 743226 |
Abstract
Covalent cross-links can be inserted between the subunits of F-actin by using p-NN'-phenylenebismaleimide. Cross-linking reaches its maximum value when one molecule of reagent has reacted with each actin subunit. p-NN'-Phenylenebismaleimide reacts initially with a cysteine residue on one subunit, the slower cross-linking reaction involving a lysine residue on a neighbouring subunit. Hydrolysis of the actin-bound reagent limits the extent of cross-linking. Quantitative analysis of the amounts of cross-linked oligomers seen on polyacrylamide gels containing sodium dodecyl sulphate suggests that neither the binding of the reagent to actin nor the formation of cross-links introduces strain into the structure. The cross-links do not join together different F-actin filaments, and evidence is presented that suggests that the cross-links join subunits of the same long-pitched helix.Entities:
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Year: 1978 PMID: 743226 PMCID: PMC1186165 DOI: 10.1042/bj1751023
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857