Literature DB >> 6254766

Dissociation of the DNAse-I . actin complex by formamide.

K Zechel.   

Abstract

Rabbit skeletal muscle actin labeled with 125 iodine by an enzymic method is shown to be capable of polymerization and to bind to matrix-bound pancreatic DNAse I like unlabeled G-actin. It was used to demonstrate that actin can be released from DNAse-I-agarose by 35--40% formamide. Actin which was only shortly exposed to this solvent was able to bind again to DNAse I and to form filaments indicating that it has been recovered functionally intact from the affinity matrix.

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Year:  1980        PMID: 6254766     DOI: 10.1111/j.1432-1033.1980.tb04872.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Construction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene.

Authors:  D Shortle; P Novick; D Botstein
Journal:  Proc Natl Acad Sci U S A       Date:  1984-08       Impact factor: 11.205

2.  Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin.

Authors:  S J Kron; D G Drubin; D Botstein; J A Spudich
Journal:  Proc Natl Acad Sci U S A       Date:  1992-05-15       Impact factor: 11.205

3.  Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces.

Authors:  J V Kilmartin; A E Adams
Journal:  J Cell Biol       Date:  1984-03       Impact factor: 10.539

  3 in total

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