Calcium‐dependent binding between calmodulin and lysozyme
- 10 April 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 247 (1) , 22-24
- https://doi.org/10.1016/0014-5793(89)81231-1
Abstract
Calmodulin, an acidic protein that binds calcium with high affinity, has multiple roles in the activation of many enzymes involved in cellular regulation of eukaryotes. In this study we show that calmodulin binding to hen egg‐white lysozyme, in a Ca2+‐dependent way, was observed using electroblots incubated with biotinylated calmodulin and detected with avidin‐alkaline phosphatase or for affinity chromatography on a gel calmodulin column. Antimicrobial activity of lysozyme was not modified in the presence of Ca2+‐calmodulin.Keywords
This publication has 17 references indexed in Scilit:
- T7 lysozyme inhibits transcription by T7 RNA polymeraseCell, 1987
- A rapid and sensitive method for detection and quantification of calcineurin and calmodulin-binding proteins using biotinylated calmodulin.Proceedings of the National Academy of Sciences, 1985
- What's new in lysozyme research?Molecular and Cellular Biochemistry, 1984
- CalmodulinAnnual Review of Biochemistry, 1980
- Calmodulin—an intracellular calcium receptorNature, 1980
- Calmodulin Plays a Pivotal Role in Cellular RegulationScience, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- [30] Activity correlations between similarly modified soluble and immobilized enzymesPublished by Elsevier ,1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The Three-Dimensional Structure of an Enzyme MoleculeScientific American, 1966