Related Experiment Video
Updated: Sep 20, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
Effects of zinc on the activity and conformational changes of arginine kinase and its intermediate
1Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Abstract:
The effects of zinc on arginine kinase and its collapsed-state intermediate were studied. Both arginine kinase and the collapsed-state intermediate were inactivated in the presence of zinc, following a biphasic kinetic course. The corresponding apparent rate constants of inactivation at different zinc concentrations and conformational changes in the presence of 0.5 mM zinc were obtained. The conformational changes of arginine kinase and the collapsed-state intermediate were followed by fluorescence spectra and circular dichroism spectra. Comparison of the results for arginine kinase and the collapsed-state intermediate showed that the collapsed-state intermediate was more susceptible to zinc, which indicated that the collapsed-state intermediate was more flexible and unstable than arginine kinase. The special structure of arginine kinase might explain these diverse phenomena.
Related Concept Videos
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Amplifying Signals via Enzymatic Cascade
EDTA: Auxiliary Complexing Reagents
The JAK-STAT Signaling Pathway
GPCRs Regulate Adenylyl Cylase Activity
Two...
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

