Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Kinetic heterogeneity of F-actin polymers. Further evidence that the elongation reaction may occur through condensation of the actin filaments with small aggregates.

Literature DB >> 3435480

Kinetic heterogeneity of F-actin polymers. Further evidence that the elongation reaction may occur through condensation of the actin filaments with small aggregates.

Abstract

We have shown that F-actin, polymerized in 50 mM-KCl at 20 degrees C and pH 8.0, can be resolved by centrifugation into two polymer populations, which differ morphologically as well as kinetically. The first population represents about 10% of the overall polymer and is composed of small amorphous aggregates. It rapidly exchanges the bound nucleotide with free ATP in the medium, either directly or through the monomers. The second population is composed of long actin filaments. These are labelled by free ATP in the medium only through condensation with labelled small amorphous aggregates.

Entities: Chemical

Mesh：

Substances：

Year: 1987 PMID： 3435480 PMCID： PMC1148609 DOI： 10.1042/bj2480721

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

17 in total

6. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors: M M Bradford
Journal: Anal Biochem Date: 1976-05-07 Impact factor: 3.365

7. Electron microscope observations on actomyosin and actin preparations from Physarum polycephalum, and on their interaction with heavy meromyosin subfragment I from muscle myosin.

Authors: V T Nachmias; H E Huxley
Journal: J Mol Biol Date: 1970-05-28 Impact factor: 5.469

Kinetic heterogeneity of F-actin polymers. Further evidence that the elongation reaction may occur through condensation of the actin filaments with small aggregates.

1. Myosin from starfish egg: properties and interaction with actin.

2. Kinetics of the cooperative association of actin to actin filaments.

3. Kinetic analysis of the polymerization process of actin.

4. F-ACTIN IS A RIGHT-HANDED HELIX.

5. Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin.

6. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

7. Electron microscope observations on actomyosin and actin preparations from Physarum polycephalum, and on their interaction with heavy meromyosin subfragment I from muscle myosin.

8. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association.

9. Separation and interaction of the major components of sea urchin actin gel.

10. The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence.

1. An alternative pathway of actin filament elongation. The condensation of small oligomers.