학술논문

Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of β-actin.
Document Type
Article
Source
European Journal of Biochemistry. Oct99 Part 1, Vol. 265 Issue 1, p210. 11p.
Subject
*GENETIC mutation
*SERINE
*ASPARAGINE
*BINDING sites
*ADENOSINE triphosphatase
Language
ISSN
0014-2956
Abstract
Analyzes the mutation of Ser14 and Asp157 in the nucleotide-binding site of beta-actin. Decrease of ATPase activity of actin in the presence of magnesium ions; Effect of profilin in the lag phases and elongation rates during polymerization of mutant actin; Hydrolysis of ATP by mutant and wild-type G-actins; Thermal stability of actin monomers; Interdomain coupling of actin.